arginine has been researched along with diacetyl in 162 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 128 (79.01) | 18.7374 |
1990's | 21 (12.96) | 18.2507 |
2000's | 10 (6.17) | 29.6817 |
2010's | 3 (1.85) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J | 1 |
Afolayan, A; Ingulli, J; Levy, HR | 1 |
Colman, RF; Ehrlich, RS | 1 |
Hemmilä, IA; Mäntsälä, PI | 1 |
Chollet, R | 2 |
Enoch, HG; Strittmatter, P | 1 |
Bodley, JW; MarSchel, AH | 2 |
Davidson, WS; Flynn, TG | 1 |
James, GT | 1 |
Michel, A; Zanen, J | 1 |
Cipollo, KL; Dunlap, RB | 1 |
Lescano, WI; Lucero, HA; Vallejos, RH | 1 |
Jordan, F; Wu, A | 1 |
Buc, H; Dreyfus, M; Vandenbunder, B | 2 |
Murphy, AJ | 1 |
Frigeri, L; Galante, YM; Hanstein, WG; Hatefi, Y | 1 |
Andreo, CS; Vallejos, RH | 1 |
Hulkower, S; Jagendorf, AT; Schmid, R | 1 |
Borders, CL; McElvany, KD; Riordan, JF | 1 |
Bonting, SL; de Pont, JJ; Schoot, BM; van Prooijen-van Eeden, A | 1 |
Fothergill, LA | 1 |
Aspiiants, RA; Benkevich, NV; Nagradova, NK | 1 |
Colman, RF; Hayman, S | 1 |
Grisham, CM | 1 |
Bragg, PD; Homyk, M | 1 |
Butterworth, PJ; Woodroofe, MN | 1 |
Rogers, K; Weber, BH | 1 |
Izui, K; Kameshita, I; Katsuki, H; Tokushige, M | 1 |
Borders, CL; George, AL; Woodall, ML | 1 |
Kameshita, I; Katsuki, H; Tokushige, M | 1 |
Londesborough, J; Varimo, K | 1 |
Riordan, JF | 1 |
Cardemil, E; Eyzaguirre, J | 1 |
Curti, B; Gozzer, C; Sacchi, G; Zanetti, G | 1 |
Chirikjian, JG; Lee, YH | 1 |
Dodgson, KS; Gacesa, P; Olavesen, AH | 1 |
Borders, CL; Zurchier, JA | 1 |
Bellini, T; Dallocchio, F; Rippa, M; Signorini, M | 1 |
Gawron, O; Jones, L | 1 |
Arvidsson, L; Hjelmgren, T; Strid, L | 1 |
Kazarinoff, MN; Snell, EE | 1 |
Crifò, C; De Marco, C; Rinaldi, A; Santoro, L | 1 |
Borchardt, RT; Schasteen, CS | 1 |
Chatagner, F; Pierre, Y | 1 |
Dietl, T; Tschesche, H | 1 |
Fliss, H; Tozer, NM; Viswanatha, T | 1 |
Nakagawa, H; Ogura, N; Sato, T; Sato, Y; Shiraishi, N | 1 |
Blaghen, M; el Kebbaj, MS; Tritsch, D; Vidon, DJ | 1 |
Desideri, A; Paci, M; Rotilio, G; Sette, M | 1 |
Brown, CA; Mahuran, DJ | 1 |
Ray, M; Ray, S; Sarkar, D | 1 |
Asryants, RA; Kuzminskaya, EV; Nagradova, NK | 1 |
Neujahr, HY; Sejlitz, T | 1 |
Prabhune, AA; Sivaraman, H | 1 |
Cheng, KC; Nowak, T | 1 |
Koyama, T; Ogura, K; Yoshida, I | 1 |
Dasarathy, Y; Fanburg, BL; Lanzillo, JJ | 1 |
Asryants, RA; Douzhenkova, IV; Kuzminskaya, EV; Nagradova, NK; Tishkov, VI | 1 |
Dekker, EE; Epperly, BR | 1 |
Koide, S; Matsuzawa, H; Miyazawa, T; Ohta, T; Yokoyama, S | 1 |
Kirkness, EF; Turner, AJ; Widdows, KB | 1 |
Di Pietro, A; Goffeau, A | 1 |
Allen, KE; Kasamo, K; Kasher, JS; Slayman, CW | 1 |
Müller, F; Visser, AJ; Wijnands, RA | 1 |
Bohren, KM; von Wartburg, JP; Wermuth, B | 1 |
Cardemil, E; Malebrán, LP | 1 |
Matthews, KS; Whitson, PA | 1 |
Holohan, PD; Ross, CR; Sokol, PP | 1 |
Dailey, HA; Fleming, JE; Harbin, BM | 1 |
Hersh, LB; Jackson, DG | 1 |
Kolattukudy, PE; Poulose, AJ | 2 |
Benjamin, RC; Cook, PF; Harris, BG; Kong, CT; Rao, GS | 1 |
Julien, T; Zaki, L | 1 |
Palmieri, F; Prezioso, G; Stipani, I; Zaki, L; Zara, V | 1 |
Church, FC; Griffith, MJ; Villanueva, GB | 1 |
Bhaduri, A; Mukherji, S | 1 |
Blech, DM; Borders, CL; Fridovich, I; Saunders, JE | 1 |
Massey, V; Nishino, T; Williams, CH | 1 |
Fushiki, T; Iwai, K; Iwami, K; Yasumoto, K | 1 |
Hernández, F; López-Rivas, A; Palacián, E; Pintor-Toro, JA; Vázquez, D | 1 |
Ivanov, KK; Kazdobina, IS; Kolesnikova, VA; Shibaeva, IV; Ugriumova, GA | 1 |
Marshall, M; Pillai, RP; Villafranca, JJ | 1 |
Bonting, SL; de Pont, JJ; Schrijen, JJ; van Amelsvoort, JM | 1 |
Myer, JP; Pande, J | 1 |
Wong, LJ; Wong, SS | 1 |
Anai, M; Nakano, I | 1 |
Berrocal, F; Carreras, J | 1 |
Belousova, LV; Moskvitina, EL; Severin, SE | 1 |
Reed, DJ; Schasteen, CS | 1 |
Kochetov, GA; Usmanov, RA | 2 |
Hochman, Y; Kenney, WC; Zakim, D | 1 |
Gomazkova, VS; Severin, SE; Stafeeva, OA | 2 |
Broquet, P; Louisot, P; Serres-Guillaumond, M | 1 |
Khailova, LS; Nemerya, NS; Severin, SE | 1 |
Bieth, JG; Davril, M; Duportail, G; Han, KK; Jung, ML; Lohez, M | 1 |
Hsu, RY; Vernon, CM | 1 |
Banaś, T; Krotkiewska, B; Marcinkowska, A; Wolny, M | 1 |
Gracy, RW; Lu, HS; Talent, JM | 1 |
Fujioka, M; Takata, Y | 1 |
Ichimura, S; Mita, K; Zama, M | 1 |
Dodgson, KS; Gacesa, P; Olavesen, AH; Savitsky, MJ | 1 |
Gripon, JC; Hofmann, T | 1 |
Cipollo, KL; Dunlap, RB; Ellis, PD; Lewis, CA | 1 |
Fox, PF; Shalabi, SI | 1 |
Asriiants, RA; Benkevich, NV; Nagradova, NK | 1 |
Campese, D; De Caro, A; Lafont, H; Lombardo, D; Multigner, L | 1 |
Mautner, HG; Merrill, RE; Pakula, AA | 1 |
Ashmarina, LI; Asryants, RA; Muronetz, VI; Nagradova, NK | 1 |
Fukui, S; Kuno, S; Toraya, T | 1 |
Kochetov, GA | 1 |
Boggaram, V; Mannervik, B | 1 |
El Kebbaj, MS; Gaudemer, Y; Latruffe, N; Moussard, C | 1 |
El Kebbaj, MS; Gaudemer, Y; Latruffe, N | 1 |
Baratova, LA; Safronova, MI; Shuvalova, ER; Vospel'nikova, ND; Zheltova, AO | 1 |
Jiang, ZY; Thorpe, C | 1 |
Maccioni, RB; Slebe, JC; Vera, JC | 1 |
Berezin, IV; Egorov, AM; Popov, VO; Tishkov, VI | 1 |
Chang, GG; Huang, TM | 1 |
Choi, JD; McCormick, DB | 1 |
Benjamin, WB; Ramakrishna, S | 1 |
Chang, GG; Chang, TC; Chueh, SH; Pan, F | 1 |
Akeroyd, R; Lange, LG; Westerman, J; Wirtz, KW | 1 |
Baratova, LA; Kniazev, SP; Nagradova, NK; Safronova, MI; Shuvalova, ER; Vospelnikova, ND | 1 |
Franks, DJ; Ngo, TT; Tunnicliff, G | 1 |
Egan, RM; Kremer, AB; Sable, HZ | 1 |
Patthy, L; Thész, J | 1 |
Egorov, AM; Popov, VO; Tishkov, VI | 1 |
Cohen, PP; Marshall, M | 1 |
Kantrowitz, ER; Vensel, LA | 1 |
el-Kebbaj, MS; Gaudemer, Y; Latruffe, N | 1 |
Terada, T | 1 |
Haeggström, JZ; Mueller, MJ; Samuelsson, B | 1 |
Ohta, T; Taguchi, H | 1 |
Billi de Catabbi, SC; San Martin de Viale, LC | 1 |
Bazaes, S; Cardemil, E; Goldie, H; Jabalquinto, AM; Silva, R | 1 |
Gutiérrez, M; Montero, C; Segura, DI | 1 |
Adak, S; Banerjee, RK; Mazumder, A | 1 |
Kevelaitis, E; Menasché, P; Mouas, C | 1 |
Ali, R; Shah, MA; Tayyab, S | 1 |
Costa, B; Giusti, L; Lucacchini, A; Martini, C | 1 |
Bernardi, P; Eriksson, O; Fontaine, E | 1 |
Davies, AH; Fann, M; Kuroda, T; Maloney, PC; Sevier, C; Tsuchiya, T; Varadhachary, A | 1 |
Borra, M; Igarashi, R; Lin, YS; Meyer, CR; Springsteel, M | 1 |
Adak, S; Bandyopadhyay, D; Bandyopadhyay, U; Banerjee, RK | 1 |
Banerjee, A; Fitzpatrick, PF; Fleming, GS; Gadda, G | 1 |
Ferry, JG; Iyer, PP | 1 |
Chen, G; Chen, X | 1 |
Garofalo, C; Gualerzi, CO; La Teana, A; Lammi, M; Petrelli, D; Pon, CL; Spurio, R | 1 |
RENDI, R | 1 |
Parker, AR | 2 |
Chang, WC; Chien, LF; Hsiao, YY; Hsu, SH; Huang, YT; Lee, CH; Liu, PF; Liu, TH; Pan, RL; Pan, YJ; Wang, YK | 1 |
Chang, HY; Lee, HJ; Peng, HL; Venkatesan, N | 1 |
Burgess, JP; Mathews, JM; Morgan, DL; Snyder, RW; Watson, SL | 1 |
Bianchini, EP; Borgel, D; Fazavana, J; Picard, V; Saller, F; Smadja, C; Taverna, M | 1 |
Dhungana, S; Fennell, TR; Morgan, DL; Waidyanatha, S; Watson, SL | 1 |
3 review(s) available for arginine and diacetyl
Article | Year |
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Arginyl residues and anion binding sites in proteins.
Topics: Anions; Arginine; Binding Sites; Biological Evolution; Chemical Phenomena; Chemistry; Cyclohexanones; Diacetyl; Guanidines; Phenylglyoxal; Phosphates; Proteins | 1979 |
Transport ATPases in anion and proton transport.
Topics: Adenosine Triphosphatases; Animals; Anions; Arginine; Biological Transport, Active; Diacetyl; Dithionitrobenzoic Acid; Erythrocyte Membrane; Kidney; Microvilli; Mitochondria; Nucleotides; Potassium; Protons; Sulfhydryl Compounds | 1980 |
Structure of the active center of transketolase.
Topics: Apoenzymes; Arginine; Binding Sites; Calcium; Diacetyl; Diethyl Pyrocarbonate; Histidine; Magnesium; Saccharomyces cerevisiae; Structure-Activity Relationship; Thiamine Pyrophosphate; Transketolase | 1982 |
159 other study(ies) available for arginine and diacetyl
Article | Year |
---|---|
Chemical genetics reveals a complex functional ground state of neural stem cells.
Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells | 2007 |
Identification of essential arginine residues in glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Topics: Amino Acids; Arginine; Butanones; Diacetyl; Fluorescence; Glucosephosphate Dehydrogenase; Glucosephosphates; Kinetics; Leuconostoc; NAD; NADP; Scattering, Radiation | 1977 |
The role of arginine in the triphosphopyridine nucleotide dependent isocitrate dehydrogenase of pig heart.
Topics: Animals; Arginine; Binding Sites; Diacetyl; Isocitrate Dehydrogenase; Myocardium; NADP; Protein Binding; Swine | 1977 |
Inactivation of glutamate dehydrogenase and glutamate synthase from Bacillus megaterium by phenylglyoxal, butane-2,3-dione and pyridoxal 5'-phosphate.
Topics: Aldehydes; Arginine; Bacillus megaterium; Binding Sites; Butanones; Diacetyl; Glutamate Dehydrogenase; Glutamate Synthase; Glyoxal; Kinetics; NADP; Pyridoxal Phosphate; Transaminases | 1978 |
Inactivation of tobacco ribulosebisphosphate carboxylase by 2,3-butanedione.
Topics: Arginine; Binding Sites; Buffers; Butanones; Carboxy-Lyases; Diacetyl; Dose-Response Relationship, Drug; Hydrogen-Ion Concentration; Kinetics; Ligands; Nicotiana; Plants, Toxic; Ribulose-Bisphosphate Carboxylase | 1978 |
Role of tyrosyl and arginyl residues in rat liver microsomal stearylcoenzyme A desaturase.
Topics: Amino Acids; Animals; Arginine; Binding Sites; Cyclohexanones; Diacetyl; Fatty Acid Desaturases; Kinetics; Microsomes, Liver; Rats; Stearoyl-CoA Desaturase; Structure-Activity Relationship; Tetranitromethane; Tyrosine | 1978 |
Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione.
Topics: Amino Acids; Arginine; Binding Sites; Borates; Butanones; Chemical Phenomena; Chemistry; Diacetyl; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Peptide Elongation Factors | 1979 |
A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney.
Topics: Aldehyde Oxidoreductases; Animals; Arginine; Diacetyl; Kidney; Kinetics; NADP; Nicotinamide Mononucleotide; Protein Binding; Pyruvaldehyde; Spectrophotometry; Swine | 1979 |
Essential arginine residues in human liver arylsulfatase A.
Topics: Arginine; Borates; Cerebroside-Sulfatase; Diacetyl; Humans; In Vitro Techniques; Liver; Phenylglyoxal; Sulfatases; Sulfites | 1979 |
[Proceedings: Chemical modification of arginyl residues of diphtheria toxin and its fragment a].
Topics: Adenosine Diphosphate; Arginine; Diacetyl; Diphtheria Toxin; HeLa Cells; Molecular Weight; Peptide Elongation Factors; Peptide Fragments; Polymers; Ribose | 1976 |
Essential arginyl residues in thymidylate synthetase.
Topics: Arginine; Binding Sites; Deoxyuracil Nucleotides; Diacetyl; Folic Acid; Kinetics; Lacticaseibacillus casei; Methyltransferases; Thymidine Monophosphate; Thymidylate Synthase | 1978 |
Involvement of an essential arginyl residue in the coupling activity of Rhodospirillum rubrum chromatophores.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Arginine; Bacterial Chromatophores; Diacetyl; Kinetics; Oxidative Phosphorylation Coupling Factors; Photophosphorylation; Rhodospirillum rubrum | 1978 |
Inactivation of purine nucleoside phosphorylase by modification of arginine residues.
Topics: Animals; Arginine; Cattle; Diacetyl; Erythrocytes; Glyoxal; Humans; Kinetics; Pentosyltransferases; Purine-Nucleoside Phosphorylase; Spleen | 1978 |
[Chemical reactivity of an essential arginine residue in substrate binding, reflecting the state of activation of glycogen phosphorylase in rabbit muscle].
Topics: Adenosine Monophosphate; Animals; Arginine; Binding Sites; Butanones; Diacetyl; Enzyme Activation; Kinetics; Muscles; Phosphorylase a; Phosphorylase b; Phosphorylases; Protein Binding; Protein Conformation; Rabbits | 1979 |
Arginyl residue modification of the sarcoplasmic reticulum ATPase protein.
Topics: Adenosine Triphosphatases; Animals; Arginine; Binding Sites; Butanones; Calcium; Diacetyl; Enzyme Activation; Kinetics; Magnesium; Muscles; Protein Binding; Rabbits; Sarcoplasmic Reticulum | 1976 |
Effects of arginine binding reagents on ATPase and ATP-Pi exchange activities of mitochondrial ATP synthetase complex (complex V).
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Aldehydes; Arginine; Binding Sites; Butanones; Diacetyl; Glyoxal; Kinetics; Mitochondria, Muscle; Oxidative Phosphorylation; Uncoupling Agents | 1977 |
An essential arginyl residue in the soluble chloroplast ATPase.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Arginine; Boric Acids; Butanones; Calcium; Chloroplasts; Diacetyl; Kinetics | 1977 |
Arginine modifiers as energy transfer inhibitors in photophosphorylation.
Topics: Aldehydes; Arginine; Borates; Buffers; Butanones; Chloroplasts; Diacetyl; Dose-Response Relationship, Drug; Edetic Acid; Electron Transport; Energy Transfer; Glyoxal; Photophosphorylation; Plants; Proton-Translocating ATPases | 1977 |
Arginyl residues: anion recognition sites in enzymes.
Topics: Adenosine Monophosphate; Allosteric Regulation; Anions; Arginine; Binding Sites; Biological Evolution; Carbohydrate Epimerases; Catalysis; Diacetyl; Fructose-Bisphosphatase; Glucose-6-Phosphate Isomerase; Glycolysis; Hexokinase; Phosphotransferases; Structure-Activity Relationship; Triose-Phosphate Isomerase | 1977 |
An essential arginine residue in the ATP-binding centre of (Na+ + K+)-ATPase.
Topics: 4-Nitrophenylphosphatase; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Arginine; Binding Sites; Diacetyl; Enzyme Activation; Kidney Medulla; Kinetics; Potassium; Protein Binding; Rabbits; Sodium | 1977 |
Reaction of yeast phosphoglycerate mutase with butanedione [proceedings].
Topics: Arginine; Binding Sites; Butanones; Diacetyl; Kinetics; Macromolecular Substances; Phosphoglycerate Mutase; Phosphotransferases; Saccharomyces cerevisiae | 1977 |
[Cooperativity of the active centers of D-glyceraldehyde-3-phosphate dehydrogenase revealed by the arginine residue modification method].
Topics: Arginine; Binding Sites; Diacetyl; Enzyme Activation; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; NAD; Substrate Specificity | 1978 |
Effect of arginine modification on the catalytic activity and allosteric activation by adenosine diphosphate of the diphosphopyridine nucleotide specific isocitrate dehydrogenase of pig heart.
Topics: Adenosine Diphosphate; Allosteric Regulation; Animals; Arginine; Butanones; Diacetyl; Enzyme Activation; Isocitrate Dehydrogenase; Kinetics; Myocardium; NAD; Swine | 1978 |
Characterization of essential arginyl residues in sheep kidney (Na+ + K+) -ATPase.
Topics: Adenosine Monophosphate; Animals; Arginine; Diacetyl; Kidney Medulla; Kinetics; Phosphates; Sheep; Sodium-Potassium-Exchanging ATPase | 1979 |
Photooxidation of NADH by 2,3-butanedione: a potential source of error in studies on active site arginyl residues.
Topics: Arginine; Butanones; Diacetyl; Light; NAD; Oxidation-Reduction | 1979 |
Evidence for the importance of arginine residues in pig kidney alkaline phosphatase.
Topics: Alkaline Phosphatase; Animals; Arginine; Diacetyl; Glyoxal; Kidney Cortex; Kinetics; Ligands; NAD; Swine | 1979 |
Evidence for an essential role for arginyl residues for yeast phosphoglycerate kinase.
Topics: Adenosine Triphosphate; Arginine; Butanones; Cyclohexanones; Diacetyl; Lysine; Magnesium; Phosphoglycerate Kinase; Saccharomyces cerevisiae | 1977 |
Reversible desensitization of phosphoenolpyruvate carboxylase to multiple effectors by butanedione.
Topics: Acetyl Coenzyme A; Allosteric Site; Arginine; Aspartic Acid; Binding Sites; Borates; Butanones; Diacetyl; Escherichia coli; Guanosine Triphosphate; Kinetics; Lactates; Lauric Acids; Magnesium; Phosphoenolpyruvate Carboxykinase (GTP) | 1977 |
Essential arginyl residues in yeast enolase.
Topics: Arginine; Diacetyl; Glycerophosphates; Kinetics; Phosphates; Phosphoenolpyruvate; Phosphopyruvate Hydratase; Saccharomyces cerevisiae | 1978 |
Phosphoenolpyruvate carboxylase of Escherichia coli. Essential arginyl residues for catalytic and regulatory functions.
Topics: Arginine; Carboxy-Lyases; Diacetyl; Escherichia coli; Kinetics; Phosphoenolpyruvate Carboxylase; Protein Binding | 1978 |
Evidence for essential arginine in yeast adenylate cyclase.
Topics: Adenosine Triphosphate; Adenylyl Cyclases; Arginine; Binding Sites; Diacetyl; Kinetics; Saccharomyces cerevisiae | 1979 |
Evidence of essential arginyl residues in rabbit muscle pyruvate kinase.
Topics: Amino Acids; Animals; Arginine; Binding Sites; Butanones; Diacetyl; Kinetics; Muscles; Pyruvate Kinase; Rabbits | 1979 |
Modification of arginyl residues in ferredoxin-NADP+ reductase from spinach leaves.
Topics: Aldehydes; Amino Acids; Arginine; Butanones; Cyclohexanes; Cyclohexanones; Diacetyl; Ferredoxin-NADP Reductase; Glyoxal; Kinetics; Ligands; NADH, NADPH Oxidoreductases; Plants | 1979 |
Sequence-specific endonuclease Bgl I. Modification of lysine and arginine residues of the homogeneous enzyme.
Topics: Arginine; Bacillus; Deoxyribonucleases; Diacetyl; Endonucleases; Kinetics; Lysine; Magnesium; Molecular Weight; Pyridoxal Phosphate | 1979 |
Functional arginine residues in bovine testicular hyaluronidase [proceedings].
Topics: Animals; Arginine; Binding Sites; Cattle; Diacetyl; Hyaluronoglucosaminidase; Kinetics; Male; Testis | 1979 |
Rabbit muscle enolase also has essential arginyl residues.
Topics: Animals; Arginine; Binding Sites; Diacetyl; Kinetics; Muscles; Phosphopyruvate Hydratase; Protein Binding; Rabbits | 1979 |
The active site of 6-phosphogluconate dehydrogenase. A phosphate binding site and its surroundings.
Topics: Arginine; Arsenates; Binding Sites; Candida; Diacetyl; Dithionitrobenzoic Acid; Histidine; Lysine; Phosphates; Phosphogluconate Dehydrogenase; Pyridoxal Phosphate; Sulfhydryl Compounds | 1978 |
Structural basis for aconitase activity inactivation by butanedione and binding of substrates and inhibitors.
Topics: Aconitate Hydratase; Aconitic Acid; Animals; Arginine; Binding Sites; Binding, Competitive; Borates; Butanones; Citrates; Diacetyl; Iron; Kinetics; Swine | 1977 |
An essential arginyl residue in phosphoglycerate kinase from yeast.
Topics: Amino Acids; Arginine; Binding Sites; Diacetyl; Kinetics; Phosphoglycerate Kinase; Protein Binding; Saccharomyces cerevisiae | 1976 |
D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site.
Topics: Apoenzymes; Arginine; Binding Sites; Diacetyl; Escherichia coli; Kinetics; L-Serine Dehydratase; Protein Binding; Pyridoxal Phosphate | 1976 |
Essential arginine residues in beef kidney D-aspartate oxidase (a preliminary report).
Topics: Amino Acid Oxidoreductases; Animals; Arginine; Aspartic Acid; Binding Sites; Cattle; Diacetyl; Glyoxal; Kidney | 1977 |
Phenol-sulfotransferase inactivation by 2,3-butanedione and phenylglyoxal: evidence for an active site arginyl residue.
Topics: Adenosine Monophosphate; Aldehydes; Animals; Arginine; Binding Sites; Butanones; Chemical Phenomena; Chemistry; Diacetyl; Dose-Response Relationship, Drug; Glyoxal; Liver; Male; Phenols; Protein Binding; Rats; Sulfurtransferases | 1977 |
Functional arginine in the active center of rat liver cystathionase.
Topics: Animals; Arginine; Binding Sites; Binding, Competitive; Cystathionine gamma-Lyase; Cysteine; Diacetyl; Homoserine; Liver; Lyases; Pyridoxal Phosphate; Rats | 1977 |
Determination of arginine in the reactive site of proteinase inhibitors by selective and reversible derivatization of the arginine side chain.
Topics: Arginine; Binding Sites; Borates; Cyclohexanones; Diacetyl; Lysine; Magnetic Resonance Spectroscopy; Molecular Weight; Spectrophotometry, Ultraviolet; Time Factors; Trypsin; Trypsin Inhibitors | 1976 |
The reaction of chymotrypsin with 2,3-butanedione trimer;.
Topics: Acridines; Amino Acids; Arginine; Binding Sites; Chymotrypsin; Diacetyl; Dioxoles; Furans; Isoflurophate; Kinetics; Light; Nitrobenzenes; Protein Binding; Temperature; Time Factors | 1975 |
Arginine and lysine residues as NADH-binding sites in NADH-nitrate reductase from spinach.
Topics: Amino Acid Sequence; Arginine; Binding Sites; Diacetyl; Humans; Lysine; Molecular Sequence Data; NAD; NADH, NADPH Oxidoreductases; Nitrate Reductase (NADH); Nitrate Reductases; Phenylglyoxal; Plants; Pyridoxal Phosphate; Sequence Homology, Nucleic Acid | 1992 |
Essential arginines in mercuric reductase isolated from Yersinia enterocolitica 138A14.
Topics: Arginine; Binding Sites; Diacetyl; Enzyme Activation; Enzyme Stability; Kinetics; NADP; Oxidoreductases; Phenylglyoxal; Yersinia enterocolitica | 1992 |
NMR evidence for perturbation of the copper coordination sphere upon chemical modification of arginine 141 in bovine Cu,Zn superoxide dismutase.
Topics: Amino Acid Sequence; Animals; Arginine; Binding Sites; Cattle; Copper; Diacetyl; Electron Spin Resonance Spectroscopy; Erythrocytes; Magnetic Resonance Spectroscopy; Superoxide Dismutase; Thermodynamics | 1991 |
Active arginine residues in beta-hexosaminidase. Identification through studies of the B1 variant of Tay-Sachs disease.
Topics: Arginine; Base Sequence; beta-N-Acetylhexosaminidases; Blotting, Western; Catalysis; Cell Line; Diacetyl; Hexosaminidase A; Hexosaminidase B; Humans; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Lysosomes; Molecular Sequence Data; Mutation; Phenylglyoxal; Tay-Sachs Disease; Transfection | 1991 |
Aminoacetone synthase from goat liver. Involvement of arginine residue at the active site and on the stability of the enzyme.
Topics: Acetyl Coenzyme A; Acetyltransferases; Animals; Arginine; Binding Sites; Diacetyl; Edetic Acid; Enzyme Activation; Enzyme Reactivators; Enzyme Stability; Glycine; Goats; Liver; Magnesium; Phenylglyoxal | 1991 |
Rabbit muscle tetrameric D-glyceraldehyde-3-phosphate dehydrogenase is locked in the asymmetric state by chemical modification of a single arginine per subunit.
Topics: Animals; Arginine; Binding Sites; Diacetyl; Enzyme Activation; Enzyme Stability; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Muscles; Protein Conformation; Rabbits | 1991 |
Arginyl residues in the NADPH-binding sites of phenol hydroxylase.
Topics: Arginine; Binding Sites; Cyclohexanones; Diacetyl; Fluorescence; Kinetics; Mixed Function Oxygenases; NADP; Phenylglyoxal | 1991 |
Evidence for involvement of arginyl residue at the catalytic site of penicillin acylase from Escherichia coli.
Topics: Arginine; Binding Sites; Diacetyl; Escherichia coli; Kinetics; Penicillin Amidase; Penicillin G; Phenylacetates; Phenylglyoxal | 1990 |
Arginine residues at the active site of avian liver phosphoenolpyruvate carboxykinase.
Topics: Animals; Arginine; Binding Sites; Carbon Dioxide; Chemical Phenomena; Chemistry; Chickens; Circular Dichroism; Cyclohexanones; Diacetyl; Electron Spin Resonance Spectroscopy; Inosine Diphosphate; Kinetics; Liver; Manganese; Phenylglyoxal; Phosphoenolpyruvate; Phosphoenolpyruvate Carboxykinase (GTP); Protein Conformation | 1989 |
Protection of hexaprenyl-diphosphate synthase of Micrococcus luteus B-P 26 against inactivation by sulphydryl reagents and arginine-specific reagents.
Topics: Aldehydes; Alkyl and Aryl Transferases; Arginine; Butanones; Chloromercuribenzoates; Cyclohexanes; Cyclohexanones; Diacetyl; Dimethylallyltranstransferase; Diphosphates; Enzyme Activation; Ethylmaleimide; Hemiterpenes; Iodoacetamide; Magnesium; Micrococcus; Organophosphorus Compounds; p-Chloromercuribenzoic Acid; Phenylglyoxal; Polyisoprenyl Phosphates; Sesquiterpenes; Sulfhydryl Reagents; Transferases | 1989 |
Detection of essential arginine in bacterial peptidyl dipeptidase-4: arginine is not the anion binding site.
Topics: Anions; Arginine; Binding Sites; Chlorides; Diacetyl; Endopeptidases; Hydrolysis; Kinetics; Phenylglyoxal; Phosphates; Protease Inhibitors; Pseudomonas; Substrate Specificity; Thiorphan | 1989 |
An examination of the role of arginine residues in the functioning of D-glyceraldehyde-3-phosphate dehydrogenase.
Topics: Animals; Arginine; Arsenates; Arsenic; Binding Sites; Butanones; Diacetyl; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; Muscles; Rabbits; Saccharomyces cerevisiae | 1989 |
Inactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione. Evidence for a catalytically essential arginine residue.
Topics: Alcohol Oxidoreductases; Arginine; Binding Sites; Butanones; Catalysis; Cyclohexanones; Diacetyl; Escherichia coli; Kinetics; NAD; Pentanones; Phenylglyoxal | 1989 |
Conformation of NAD+ bound to allosteric L-lactate dehydrogenase activated by chemical modification.
Topics: Allosteric Regulation; Allosteric Site; Arginine; Butanones; Diacetyl; Fructosediphosphates; Hexosediphosphates; Kinetics; L-Lactate Dehydrogenase; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; NAD; Thermus | 1989 |
Modification of the GABA/benzodiazepine receptor with the arginine reagent, 2,3-butanedione.
Topics: Animals; Arginine; Butanones; Cerebral Cortex; Diacetyl; Kinetics; Muscimol; Receptors, GABA-A; Swine; Synaptic Membranes | 1987 |
Essential arginyl residues in the H+-translocating ATPase of plasma membrane from the yeast Schizosaccharomyces pombe.
Topics: Arginine; Ascomycota; Cell Membrane; Chemical Phenomena; Chemistry; Diacetyl; Magnesium; Proton-Translocating ATPases; Schizosaccharomyces | 1985 |
Characterization of an essential arginine residue in the plasma membrane H+-ATPase of Neurospora crassa.
Topics: Arginine; Binding Sites; Diacetyl; Kinetics; Neurospora; Neurospora crassa; Phenylglyoxal; Protein Binding; Proton-Translocating ATPases; Ribonucleotides | 1986 |
Chemical modification of arginine residues in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens: a kinetic and fluorescence study.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Arginine; Binding Sites; Diacetyl; Flavin-Adenine Dinucleotide; Fluorescence; Kinetics; Mathematics; Mixed Function Oxygenases; NADP; Phenylglyoxal; Pseudomonas fluorescens | 1987 |
Inactivation of carbonyl reductase from human brain by phenylglyoxal and 2,3-butanedione: a comparison with aldehyde reductase and aldose reductase.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Aldehyde Reductase; Aldehydes; Arginine; Brain; Butanones; Diacetyl; Humans; Kinetics; Lysine; NADP; Phenylglyoxal; Sugar Alcohol Dehydrogenases; Sulfhydryl Compounds | 1987 |
The presence of functional arginine residues in phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae.
Topics: Adenosine Diphosphate; Aldehydes; Arginine; Butanones; Chemical Phenomena; Chemistry; Diacetyl; Kinetics; Manganese; Phenylglyoxal; Phosphoenolpyruvate; Phosphoenolpyruvate Carboxykinase (GTP); Saccharomyces cerevisiae | 1987 |
Chemical modification of arginine residues in the lactose repressor.
Topics: Aldehydes; Arginine; Butanones; Diacetyl; DNA; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Phenylglyoxal; Repressor Proteins; Transcription Factors | 1987 |
Arginyl and histidyl groups are essential for organic anion exchange in renal brush-border membrane vesicles.
Topics: Aldehydes; Animals; Arginine; Butanones; Diacetyl; Diethyl Pyrocarbonate; Dithiothreitol; Dogs; Formates; Histidine; Hydroxylamine; Hydroxylamines; Kidney Cortex; Kinetics; Microvilli; p-Aminohippuric Acid; Phenylglyoxal | 1988 |
Ferrochelatase from Rhodopseudomonas sphaeroides: substrate specificity and role of sulfhydryl and arginyl residues.
Topics: Arginine; Diacetyl; Ferrochelatase; Kinetics; Lyases; Rhodobacter sphaeroides; Substrate Specificity; Sulfhydryl Compounds | 1986 |
Reaction of neutral endopeptidase 24.11 (enkephalinase) with arginine reagents.
Topics: Aldehydes; Animals; Arginine; Butanones; Diacetyl; Endopeptidases; Enkephalin, Methionine; Kidney; Kinetics; Neprilysin; Phenylglyoxal; Protease Inhibitors; Rats | 1986 |
Enzymatic reduction of phenylglyoxal and 2,3-butanedione, two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase.
Topics: 3-Oxoacyl-(Acyl-Carrier-Protein) Reductase; Alcohol Oxidoreductases; Aldehydes; Arginine; Butanones; Diacetyl; Fatty Acid Synthases; Kinetics; Oxidation-Reduction; Phenylglyoxal | 1986 |
Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suum.
Topics: Animals; Arginine; Ascaris; Binding Sites; Borates; Diacetyl; Dialysis; Hydrogen-Ion Concentration; Kinetics; Malate Dehydrogenase | 1987 |
New evidence for the essential role of arginine residues in anion transport across the red blood cell membrane.
Topics: Anion Transport Proteins; Arginine; Butanones; Carrier Proteins; Chlorides; Diacetyl; Erythrocyte Membrane; Humans; Hydrogen-Ion Concentration; Kinetics; Sulfates | 1987 |
Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific reagents.
Topics: Animals; Arginine; Binding Sites; Carrier Proteins; Citrates; Cyclohexanones; Diacetyl; Hydrogen-Ion Concentration; Liposomes; Membrane Proteins; Mitochondria, Liver; Phenylglyoxal; Protein Binding; Rats | 1986 |
Structure-function relationships in heparin cofactor II: chemical modification of arginine and tryptophan and demonstration of a two-domain structure.
Topics: Amino Acids; Antithrombin III; Arginine; Binding Sites; Bromosuccinimide; Chromatography; Circular Dichroism; Diacetyl; Glycoproteins; Guanidine; Guanidines; Heparin Cofactor II; Kinetics; Protein Denaturation; Structure-Activity Relationship; Tryptophan | 1986 |
UDP-glucose 4-epimerase from Saccharomyces fragilis. Presence of an essential arginine residue at the substrate-binding site of the enzyme.
Topics: Arginine; Binding Sites; Binding, Competitive; Carbohydrate Epimerases; Carbon Radioisotopes; Cyclohexanones; Diacetyl; Kinetics; Phenylglyoxal; Protein Binding; Saccharomyces; Spectrometry, Fluorescence; UDPglucose 4-Epimerase; Uracil Nucleotides | 1986 |
Essentiality of the active-site arginine residue for the normal catalytic activity of Cu,Zn superoxide dismutase.
Topics: Arginine; Binding Sites; Cyanides; Diacetyl; Electrophoresis, Polyacrylamide Gel; Phenylglyoxal; Superoxide Dismutase | 1985 |
Chemical modifications of D-amino acid oxidase. Evidence for active site histidine, tyrosine, and arginine residues.
Topics: Animals; Arginine; D-Amino-Acid Oxidase; Diacetyl; Diethyl Pyrocarbonate; Dinitrofluorobenzene; Histidine; Hydroxylamines; Kidney; Kinetics; Spectrophotometry; Swine; Tyrosine | 1980 |
Evidence for an essential arginyl residue in bovine milk gamma-glutamyltransferase.
Topics: Amino Acids; Animals; Arginine; Binding Sites; Butanones; Cattle; Chemical Phenomena; Chemistry; Diacetyl; gamma-Glutamyltransferase; Milk | 1983 |
Implication of arginyl residues in mRNA binding to ribosomes.
Topics: Arginine; Bacterial Proteins; Diacetyl; Escherichia coli; Phenylglyoxal; Poly U; Protein Binding; Ribosomal Proteins; Ribosomes; RNA, Bacterial; RNA, Messenger | 1980 |
[Role of arginine and histidine residues in the biological activity of botulinic neurotoxin A].
Topics: Animals; Arginine; Botulinum Toxins; Cyclohexanones; Diacetyl; Diethyl Pyrocarbonate; Epitopes; Histidine; Protein Conformation | 1983 |
Modification of an essential arginine of carbamate kinase.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Arginine; Binding Sites; Carbamates; Diacetyl; Enterococcus faecalis; Magnesium; Manganese; Phosphotransferases; Phosphotransferases (Carboxyl Group Acceptor) | 1980 |
The arginines of cytochrome c. The reduction-binding site for 2,3-butanedione and ascorbate.
Topics: Animals; Arginine; Ascorbic Acid; Binding Sites; Butanones; Cytochrome c Group; Diacetyl; Horses; Myocardium; Oxidation-Reduction; Protein Binding; Spectrophotometry | 1980 |
Evidence for an essential arginine residue at the active site of Escherichia coli acetate kinase.
Topics: Acetate Kinase; Adenine Nucleotides; Arginine; Binding Sites; Catalysis; Diacetyl; Escherichia coli; Kinetics; Phenylglyoxal; Phosphotransferases | 1981 |
Inactivation of ATP-dependent deoxyribonuclease of Micrococcus luteus by 2,3-butanedione.
Topics: Arginine; Bacterial Proteins; Butanones; Chemical Phenomena; Chemistry; Diacetyl; Exodeoxyribonuclease V; Exodeoxyribonucleases; Micrococcus; Receptors, Cell Surface; Receptors, Purinergic | 1982 |
Metabolism of glycerate-2,3-P2-III. Arginine-specific reagents inactivate the phosphoglycerate mutase, glycerate-2,3-P2 synthase and glycerate-2,3-P2 phosphatase activities of rabbit muscle phosphoglycerate mutase.
Topics: Animals; Arginine; Cyclohexanones; Diacetyl; Glyoxal; Hydroxylamine; Hydroxylamines; Muscles; Phenylglyoxal; Phosphoglycerate Mutase; Phosphoric Monoester Hydrolases; Phosphotransferases; Pyruvaldehyde; Rabbits | 1983 |
Essential arginine residues of creatine kinase from beef heart mitochondria.
Topics: Adenosine Triphosphate; Animals; Arginine; Cattle; Creatine Kinase; Cytoplasm; Diacetyl; In Vitro Techniques; Kinetics; Mitochondria, Heart; Muscles | 1983 |
Involvement of arginine residues in glutathione binding to yeast glyoxalase I.
Topics: Arginine; Camphor; Diacetyl; Dithiothreitol; Glutathione; Glutathione Disulfide; Kinetics; Lactoylglutathione Lyase; Lyases; Phenylglyoxal; Saccharomyces cerevisiae | 1983 |
[Function of the arginine residue in the active center of baker's yeast transketolase].
Topics: Arginine; Binding Sites; Butanones; Circular Dichroism; Diacetyl; Kinetics; Protein Conformation; Saccharomyces cerevisiae; Transketolase | 1983 |
Interaction of baker's yeast transketolase modified by 2,3-butanedione with anionic and nonanionic substrates.
Topics: Anions; Apoenzymes; Apoproteins; Arginine; Butanones; Circular Dichroism; Diacetyl; Fructosephosphates; Phosphorylation; Saccharomyces cerevisiae; Structure-Activity Relationship; Substrate Specificity; Thiamine Pyrophosphate; Transketolase | 1983 |
Evidence for an active site arginine in UDP-glucuronyltransferase.
Topics: Amino Acids; Animals; Arginine; Binding Sites; Butanones; Diacetyl; Glucuronates; Glucuronic Acid; Glucuronosyltransferase; Kinetics; Microsomes, Liver; Swine; Uridine Diphosphate; Uridine Diphosphate Glucuronic Acid | 1983 |
Essential arginine residues for catalytic and regulatory functions of alpha-ketoglutarate dehydrogenase from pigeon breast muscle.
Topics: Animals; Arginine; Catalysis; Columbidae; Diacetyl; In Vitro Techniques; Ketoglutarate Dehydrogenase Complex; Ketone Oxidoreductases; Kinetics; Lysine; Muscles; Pentanones | 1983 |
Involvement of some amino acid residues in the enzymatic activity of solubilized cerebral fucosyltransferase.
Topics: Animals; Arginine; Binding Sites; Brain; Butanones; Diacetyl; Diethyl Pyrocarbonate; Formates; Fucosyltransferases; Hexosyltransferases; Histidine; Hydroxylamine; Hydroxylamines; Kinetics; Methane; Sheep; Tetranitromethane; Tyrosine | 1984 |
Arginine residues in the active centers of muscle pyruvate dehydrogenase.
Topics: Animals; Arginine; Binding Sites; Columbidae; Diacetyl; Kinetics; Muscles; Phenylglyoxal; Pyruvate Dehydrogenase Complex | 1984 |
Arginine modification in elastase. Effect on catalytic activity and conformation of the calcium-binding site.
Topics: Animals; Arginine; Calcium; Cyclohexanones; Diacetyl; Hydroxylamine; Hydroxylamines; Kinetics; Pancreas; Pancreatic Elastase; Phenylglyoxal; Protein Conformation; Swine | 1984 |
Pigeon liver malic enzyme: involvement of an arginyl residue at the binding site for malate and its analogs.
Topics: Aldehydes; Animals; Arginine; Binding Sites; Butanones; Columbidae; Diacetyl; Liver; Malate Dehydrogenase; Malates; NADP; Phenylglyoxal; Spectrometry, Fluorescence | 1983 |
Localization of arginyl residues modified with butanedione in glyceraldehyde-3-phosphate dehydrogenase from pig muscle.
Topics: Animals; Arginine; Chemical Phenomena; Chemistry; Diacetyl; Glyceraldehyde-3-Phosphate Dehydrogenases; In Vitro Techniques; Muscles; Peptide Fragments; Swine | 1983 |
Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginyl residues. Physicochemical and kinetic studies.
Topics: Adenosine Monophosphate; Allosteric Regulation; Arginine; Butanones; Diacetyl; Kinetics; Phosphorylase a; Phosphorylase b; Phosphorylases; Protein Binding | 1980 |
Chemical modification of critical catalytic residues of lysine, arginine, and tryptophan in human glucose phosphate isomerase.
Topics: Affinity Labels; Arginine; Bromosuccinimide; Circular Dichroism; Cyclohexanones; Diacetyl; Female; Glucose-6-Phosphate Isomerase; Humans; Kinetics; Lysine; Molecular Weight; Placenta; Pregnancy; Protein Binding; Protein Conformation; Pyridoxal Phosphate; Tryptophan | 1981 |
Role of arginine residue in saccharopine dehydrogenase (L-lysine forming) from baker's yeast.
Topics: Amino Acids; Arginine; Diacetyl; Hydrogen-Ion Concentration; Kinetics; Lysine; Oxidoreductases Acting on CH-NH Group Donors; Saccharomyces cerevisiae; Saccharopine Dehydrogenases | 1981 |
Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1.
Topics: Animals; Arginine; Cattle; Diacetyl; Histones; Lysine; Methylurea Compounds; Thymus Gland | 1981 |
Modification of functional arginine residues in purified bovine testicular hyaluronidase with butane-2, 3-dione.
Topics: Animals; Arginine; Butanones; Cattle; Chemical Phenomena; Chemistry; Chondroitin Sulfates; Diacetyl; Enzyme Activation; Hyaluronic Acid; Hyaluronoglucosaminidase; Hydrogen-Ion Concentration; Kinetics; Male; Osmolar Concentration; Sodium Chloride; Testis | 1981 |
Inactivation of aspartyl proteinases by butane-2,3-dione. Modification of tryptophan and tyrosine residues and evidence against reaction of arginine residues.
Topics: Amino Acids; Arginine; Aspartic Acid Endopeptidases; Binding Sites; Butanones; Diacetyl; Endopeptidases; Enzyme Activation; Penicillium; Pepsin A; Protease Inhibitors; Spectrum Analysis; Tryptophan; Tyrosine | 1981 |
Carbon 13 nuclear magnetic resonance studies of Lactobacillus casei thymidylate synthetase containing biosynthetically incorporated [guanidino-13C]arginine.
Topics: Arginine; Carbon Isotopes; Diacetyl; Lacticaseibacillus casei; Magnetic Resonance Spectroscopy; Methyltransferases; Protein Conformation; Thymidylate Synthase | 1982 |
Heat stability of milk: influence of modification of lysine and arginine on the heat stability-pH profile.
Topics: Acetic Anhydrides; Aldehydes; Animals; Arginine; Butanones; Cattle; Cyclohexanes; Cyclohexanones; Dansyl Compounds; Diacetyl; Glyoxal; Hot Temperature; Hydrogen-Ion Concentration; Lysine; Methylurea Compounds; Milk | 1982 |
[Modification of arginine residues of glyceraldehyde 3-phosphate dehydrogenase. The enzyme from rat and rabbit skeletal muscles].
Topics: Animals; Arginine; Butanones; Diacetyl; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; Muscles; NAD; Rabbits; Rats; Species Specificity | 1983 |
On the probable involvement of arginine residues in the bile-salt-binding site of human pancreatic carboxylic ester hydrolase.
Topics: Amino Acids; Arginine; Bile Acids and Salts; Binding Sites; Binding, Competitive; Carboxylic Ester Hydrolases; Catalysis; Diacetyl; Enzyme Activation; Humans; Pancreas; Protein Binding | 1983 |
Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.
Topics: Acetyl Coenzyme A; Animals; Arginine; Binding Sites; Camphor; Choline O-Acetyltransferase; Decapodiformes; Diacetyl; Phenylglyoxal; Stereoisomerism | 1981 |
Presence of one essential arginine that specifically binds the 2'-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetase.
Topics: 3-Oxoacyl-(Acyl-Carrier-Protein) Reductase; Acyl Carrier Protein; Adenine Nucleotides; Alcohol Oxidoreductases; Arginine; Binding Sites; Diacetyl; Fatty Acid Desaturases; Fatty Acid Synthases; Keto Acids; Macromolecular Substances; NADP; Phenylglyoxal | 1980 |
Use of immobilized enzymatically active monomers of glyceraldehyde-3-phosphate dehydrogenase to investigate subunit cooperativity in the oligomeric enzyme.
Topics: Animals; Arginine; Diacetyl; Enzymes, Immobilized; Glyceraldehyde-3-Phosphate Dehydrogenases; Macromolecular Substances; NAD; Protein Conformation; Rats; Saccharomyces cerevisiae | 1980 |
Coenzyme B12-dependent diol dehydrase: chemical modification with 2,3-butanedione and phenylglyoxal.
Topics: Aldehydes; Arginine; Binding Sites; Butanones; Chemical Phenomena; Chemistry; Cobamides; Diacetyl; Hydro-Lyases; Klebsiella pneumoniae; Phenylglyoxal; Propanediol Dehydratase | 1980 |
Inactivation of Escherichia coli elongation factor Tu by the arginine-specific reagent butanedione.
Topics: Arginine; Bacterial Proteins; Binding Sites; Butanones; Diacetyl; Escherichia coli; Guanosine Diphosphate; Kinetics; Peptide Elongation Factor Tu; Peptide Elongation Factors | 1980 |
Essential arginine residues in the pyridine nucleotide binding sites of glutathione reductase.
Topics: Adenine Nucleotides; Arginine; Binding Sites; Diacetyl; Erythrocytes; Glutathione; Glutathione Disulfide; Glutathione Reductase; Humans; Kinetics; NADP; Phenylglyoxal; Spectrum Analysis | 1982 |
Permeability of inner mitochondrial membrane to arginine reagents.
Topics: Animals; Arginine; Cyclohexanones; Diacetyl; Hydroxybutyrate Dehydrogenase; In Vitro Techniques; Intracellular Membranes; Membrane Proteins; Mitochondria; Permeability; Phenylglyoxal; Pyruvaldehyde; Rats; Submitochondrial Particles | 1982 |
Comparative titration of arginyl residues in purified D-beta-hydroxybutyrate apodehydrogenase and in the reconstituted phospholipid-enzyme complex.
Topics: Amino Acids; Animals; Apoenzymes; Arginine; Cyclohexanones; Diacetyl; Hydroxybutyrate Dehydrogenase; Kinetics; Membrane Lipids; Mitochondria; Mitochondria, Liver; Phenylglyoxal; Phospholipids; Rats; Submitochondrial Particles | 1982 |
[Structure of glyceraldehyde-3-phosphate dehydrogenase from rat muscle. Localization of arginine residues modified by 2,3-butanedione].
Topics: Amino Acid Sequence; Animals; Arginine; Butanones; Diacetyl; Drug Stability; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; Protein Binding; Rats | 1982 |
Modification of an arginine residue in pig kidney general acyl-coenzyme A dehydrogenase by cyclohexane-1,2-dione.
Topics: Acyl Coenzyme A; Acyl-CoA Dehydrogenase; Acyl-CoA Dehydrogenases; Animals; Arginine; Binding Sites; Cyclohexanes; Cyclohexanones; Diacetyl; Fatty Acids; Kidney; Phenylglyoxal; Swine | 1982 |
Arginyl residues involvement in the microtubule assembly.
Topics: Animals; Arginine; Diacetyl; Kinetics; Microtubules; Polymers; Swine | 1981 |
Inactivation of crystalline tobacco ribulosebisphosphate carboxylase by modification of arginine residues with 2,3-butanedione and phenylglyoxal.
Topics: Aldehydes; Arginine; Binding Sites; Butanones; Carboxy-Lyases; Diacetyl; Nicotiana; Phenylglyoxal; Plants, Toxic; Ribulose-Bisphosphate Carboxylase | 1981 |
Study of the role of arginine residues in bacterial formate dehydrogenase.
Topics: Alcaligenes; Aldehyde Oxidoreductases; Amino Acids; Arginine; Azides; Diacetyl; Formate Dehydrogenases; Formates; NAD | 1981 |
Modification of essential arginine residues of pigeon liver malic enzyme.
Topics: Animals; Arginine; Columbidae; Diacetyl; Kinetics; Liver; Malate Dehydrogenase; NADP; Pentanones; Phenylglyoxal; Protein Binding; Pyruvaldehyde | 1981 |
Roles of arginyl residues in pyridoxamine-5'-phosphate oxidase from rabbit liver.
Topics: Amino Acids; Animals; Arginine; Diacetyl; Liver; Oxidoreductases Acting on CH-NH Group Donors; Pentanones; Phenylglyoxal; Pyridoxaminephosphate Oxidase; Rabbits | 1981 |
Evidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver.
Topics: Animals; Arginine; ATP Citrate (pro-S)-Lyase; Binding Sites; Citrates; Citric Acid; Coenzyme A; Diacetyl; Kinetics; Ligands; Liver; Phenylglyoxal; Rats | 1981 |
Involvement of arginine residue in the phosphate binding site of human placental alkaline phosphatase.
Topics: Alkaline Phosphatase; Arginine; Binding Sites; Diacetyl; Female; Humans; In Vitro Techniques; Kinetics; Phenylglyoxal; Phosphates; Placenta; Pregnancy; Pyruvaldehyde | 1981 |
Modification of the phosphatidylcholine-transfer protein from bovine liver with butanedione and phenylglyoxal. Evidence for one essential arginine residue.
Topics: Aldehydes; Androgen-Binding Protein; Animals; Arginine; Butanones; Carrier Proteins; Cattle; Chemical Phenomena; Chemistry; Diacetyl; Dose-Response Relationship, Drug; Kinetics; Liver; Phenylglyoxal; Phospholipid Transfer Proteins; Structure-Activity Relationship | 1981 |
Identification of an arginine residue important for catalytic activity in the primary structure of D-glyceraldehyde 3-phosphate dehydrogenase. Studies with the rat skeletal-muscle enzyme.
Topics: Amino Acid Sequence; Amino Acids; Animals; Arginine; Catalysis; Chromatography, Gel; Diacetyl; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; Peptide Fragments; Rats; Trypsin | 1981 |
Inactivation of adenylate cyclase by phenylglyoxal and other dicarbonyls. Evidence for existence of essential arginyl residues.
Topics: Adenylyl Cyclase Inhibitors; Aldehydes; Animals; Arginine; Binding Sites; Brain; Cyclohexanones; Diacetyl; Glyoxal; Male; Phenylglyoxal; Rats | 1980 |
The active site of transketolase. Two arginine residues are essential for activity.
Topics: Arginine; Binding Sites; Diacetyl; Kinetics; Phenylglyoxal; Transketolase | 1980 |
[Modification of arginine residues of alpha-ketoglutarate dehydrogenase by 2,3-butanedione].
Topics: Animals; Arginine; Binding Sites; Chemical Phenomena; Chemistry; Circular Dichroism; Columbidae; Diacetyl; Ketoglutarate Dehydrogenase Complex; Ketone Oxidoreductases; Muscles; Protein Binding; Spectrum Analysis | 1980 |
Origin of the selectivity of alpha-dicarbonyl reagents for arginyl residues of anion-binding sites.
Topics: Anions; Arginine; Binding Sites; Cyclohexanones; Diacetyl; Fructose-Bisphosphate Aldolase; Indicators and Reagents; Ketones; Phenylglyoxal | 1980 |
[Role of amino acid arginine residues of bacterial formate dehydrogenase].
Topics: Aldehyde Oxidoreductases; Amino Acids; Arginine; Bacteria; Binding Sites; Butanones; Diacetyl; Formate Dehydrogenases; Kinetics; Protein Binding | 1980 |
Evidence for an exceptionally reactive arginyl residue at the binding site for carbamyl phosphate in bovine ornithine transcarbamylase.
Topics: Amino Acids; Animals; Arginine; Binding Sites; Carbamates; Carbamyl Phosphate; Cattle; Diacetyl; Kinetics; Liver; Mathematics; Ornithine Carbamoyltransferase; Phenylglyoxal; Protein Binding; Valine | 1980 |
An essential arginine residue in porcine phospholipiase A2.
Topics: Aldehydes; Animals; Arginine; Binding Sites; Calcium; Cyclohexanones; Diacetyl; Hydrogen-Ion Concentration; Kinetics; Pancreas; Phenylglyoxal; Phosphatidylcholines; Phospholipases; Phospholipases A; Protein Binding; Structure-Activity Relationship; Swine | 1980 |
Presence of an essential arginyl residue in D-beta-hydroxybutyrate dehydrogenase from mitochondrial inner membrane.
Topics: Animals; Arginine; Cyclohexanones; Diacetyl; Hydroxybutyrate Dehydrogenase; Intracellular Membranes; Kinetics; Mitochondria, Liver; Phenylglyoxal; Protein Binding; Rats | 1980 |
Role of arginine residues of bovine liver dihydrodiol dehydrogenase 2 in the binding of anionic substrates.
Topics: Animals; Anions; Arginine; Borates; Carboxylic Acids; Cattle; Diacetyl; Enzyme Activation; Ions; Kinetics; Oxidoreductases; Protein Binding | 1995 |
Chemical modification of leukotriene A4 hydrolase. Indications for essential tyrosyl and arginyl residues at the active site.
Topics: Arginine; Binding Sites; Diacetyl; Epoxide Hydrolases; Imidazoles; Phenylglyoxal; Sulfhydryl Reagents; Tetranitromethane; Tyrosine | 1995 |
Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.
Topics: Arginine; Base Sequence; Binding Sites; Binding, Competitive; Catalysis; Diacetyl; Glutamine; Histidine; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Lactobacillus; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Substrate Specificity | 1994 |
Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. In vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens.
Topics: Animals; Arginine; Binding Sites; Carboxy-Lyases; Decarboxylation; Diacetyl; Female; Hexachlorobenzene; Histidine; Liver; Porphyrias; Porphyrinogens; Rats; Rats, Wistar | 1994 |
Reactivity of cysteinyl, arginyl, and lysyl residues of Escherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents.
Topics: Arginine; Binding Sites; Cysteine; Diacetyl; Escherichia coli; Glyoxal; Kinetics; Lysine; Phosphoenolpyruvate Carboxykinase (GTP); Pyrenes; Pyridoxal Phosphate; Sulfhydryl Reagents | 1993 |
Diacetyl for blocking the histochemical reaction for arginine.
Topics: Arginine; Barium Compounds; Diacetyl; Guanidines; Histocytochemistry; Humans; Hydrogen-Ion Concentration; Phenylglyoxal; Pituitary Gland; Tissue Fixation | 1994 |
Probing the active site residues in aromatic donor oxidation in horseradish peroxidase: involvement of an arginine and a tyrosine residue in aromatic donor binding.
Topics: Arginine; Binding Sites; Carbon Radioisotopes; Circular Dichroism; Cyclohexanones; Diacetyl; Enzyme Inhibitors; Heme; Horseradish Peroxidase; Kinetics; Models, Structural; Phenylglyoxal; Protein Structure, Secondary; Spectrophotometry; Tetranitromethane; Thermodynamics; Tyrosine | 1996 |
Poststorage diastolic abnormalities of heart transplants: is vascular dysfunction or myocardial contracture the culprit?
Topics: Animals; Arginine; Bicarbonates; Calcium Chloride; Cardiac Volume; Cardioplegic Solutions; Cholinesterase Reactivators; Coronary Circulation; Diacetyl; Diastole; Disaccharides; Electrolytes; Endothelium, Vascular; Glutamates; Glutathione; Heart Transplantation; Histidine; Magnesium; Male; Mannitol; Myocardial Contraction; Organ Preservation; Papaverine; Potassium Chloride; Rats; Rats, Sprague-Dawley; Reperfusion; Serotonin; Serotonin Receptor Agonists; Sodium Chloride; Vasodilator Agents; Ventricular Function, Left; Ventricular Pressure | 1996 |
Probing structure-activity relationship in diamine oxidase--reactivities of lysine and arginine residues.
Topics: Amine Oxidase (Copper-Containing); Arginine; Diacetyl; Lysine; Phenylglyoxal; Protein Conformation; Structure-Activity Relationship; Thermodynamics; Time Factors; Trinitrobenzenesulfonic Acid | 1996 |
2,3-Butanedione inactivates the [3H]nitrendipine binding sites, whereas diethylpyrocarbonate does not.
Topics: Animals; Arginine; Binding Sites; Brain; Calcium Channels; Diacetyl; Diethyl Pyrocarbonate; Histidine; Membranes; Nitrendipine; Protein Conformation; Rabbits; Radioligand Assay; Tritium | 1996 |
Chemical modification of arginines by 2,3-butanedione and phenylglyoxal causes closure of the mitochondrial permeability transition pore.
Topics: Animals; Arginine; Diacetyl; Intracellular Membranes; Male; Mitochondria, Liver; Permeability; Phenylglyoxal; Rats; Rats, Wistar | 1998 |
Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Bacterial Proteins; Carrier Proteins; Conserved Sequence; Diacetyl; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Sugar Phosphates | 1998 |
Characterization of ADP-glucose pyrophosphorylase from Rhodobacter sphaeroides 2.4.1: evidence for the involvement of arginine in allosteric regulation.
Topics: Allosteric Regulation; Amino Acid Sequence; Arginine; Base Sequence; Diacetyl; DNA Primers; Genes, Bacterial; Glucose-1-Phosphate Adenylyltransferase; Indicators and Reagents; Kinetics; Molecular Sequence Data; Nucleotidyltransferases; Polymerase Chain Reaction; Rhodobacter sphaeroides; Sequence Homology, Amino Acid | 1999 |
An essential role of active site arginine residue in iodide binding and histidine residue in electron transfer for iodide oxidation by horseradish peroxidase.
Topics: Arginine; Binding Sites; Carbon Radioisotopes; Circular Dichroism; Cyclohexanones; Diacetyl; Diethyl Pyrocarbonate; Electron Transport; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Iodides; Kinetics; Oxidation-Reduction; Phenylglyoxal; Spectrophotometry; Thermodynamics | 2001 |
Evidence for an essential arginine in the flavoprotein nitroalkane oxidase.
Topics: Arginine; Binding, Competitive; Cyclohexanones; Diacetyl; Dioxygenases; Enzyme Inhibitors; Flavoproteins; Fusarium; Kinetics; Oxygenases; Pentanoic Acids; Phenylglyoxal; Substrate Specificity | 2001 |
Role of arginines in coenzyme A binding and catalysis by the phosphotransacetylase from Methanosarcina thermophila.
Topics: Arginine; Catalysis; Coenzyme A; Diacetyl; Genetic Variation; Kinetics; Methanosarcina; Molecular Structure; Phosphate Acetyltransferase | 2001 |
Arginine residues in the active site of human phenol sulfotransferase (SULT1A1).
Topics: Amino Acids; Animals; Arginine; Arylsulfotransferase; Binding Sites; Catalysis; Diacetyl; DNA, Complementary; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Humans; Hydrogen-Ion Concentration; Kinetics; Methylene Blue; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Naphthols; Phenol; Phosphoadenosine Phosphosulfate; Protein Binding; Protein Isoforms; Rats; Software; Substrate Specificity; Sulfotransferases; Time Factors | 2003 |
Mapping the active sites of bacterial translation initiation factor IF3.
Topics: Arginine; Binding Sites; Diacetyl; Escherichia coli; Escherichia coli Proteins; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Peptide Chain Initiation, Translational; Prokaryotic Initiation Factor-3; Protein Binding; Protein Structure, Tertiary; Protein Subunits; Ribosomes; RNA, Messenger | 2003 |
[Colorimetric determine of arginine with diacetyl monoxime].
Topics: Arginine; Colorimetry; Diacetyl; Hydroxylamines | 1957 |
A single arginine residue is required for the interaction of the electron transferring flavoprotein (ETF) with three of its dehydrogenase partners.
Topics: Acyl-CoA Dehydrogenase; Animals; Arginine; Binding Sites; Diacetyl; Dimethylglycine Dehydrogenase; Electron Transport; Electron-Transferring Flavoproteins; Electrons; Kinetics; Oxidoreductases; Oxidoreductases, N-Demethylating; Protein Binding; Sarcosine Dehydrogenase; Swine; Time Factors | 2003 |
Binding of the human "electron transferring flavoprotein" (ETF) to the medium chain acyl-CoA dehydrogenase (MCAD) involves an arginine and histidine residue.
Topics: Acyl-CoA Dehydrogenase; Arginine; Binding Sites; Diacetyl; Diethyl Pyrocarbonate; Electron-Transferring Flavoproteins; Histidine; Humans; Protein Binding; Protein Conformation; Sequence Homology, Amino Acid; Spectrophotometry | 2003 |
Functional roles of arginine residues in mung bean vacuolar H+-pyrophosphatase.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Diacetyl; Fabaceae; Hydrogen-Ion Concentration; Hydrolysis; Hydrophobic and Hydrophilic Interactions; Inorganic Pyrophosphatase; Intracellular Membranes; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phenylglyoxal; Trypsin; Vacuoles | 2007 |
Identification of amino acid residues important for the phosphomannose isomerase activity of PslB in Pseudomonas aeruginosa PAO1.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Bacterial Proteins; Catalysis; Catalytic Domain; Cobalt; Diacetyl; DNA Mutational Analysis; Enzyme Inhibitors; Guanosine Diphosphate Mannose; Mannose-6-Phosphate Isomerase; Molecular Sequence Data; Mutation; Pseudomonas aeruginosa | 2008 |
Reaction of the butter flavorant diacetyl (2,3-butanedione) with N-α-acetylarginine: a model for epitope formation with pulmonary proteins in the etiology of obliterative bronchiolitis.
Topics: Arginine; Bronchiolitis Obliterans; Butter; Diacetyl; Flavoring Agents; Humans; Mass Spectrometry; Models, Chemical | 2010 |
A chemically-modified inactive antithrombin as a potent antagonist of fondaparinux and heparin anticoagulant activity.
Topics: Animals; Anticoagulants; Antithrombins; Arginine; Diacetyl; Drug Design; Female; Fondaparinux; Hemorrhage; Heparin; Heparin Antagonists; Humans; Mass Spectrometry; Mice; Partial Thromboplastin Time; Polysaccharides; Recombinant Proteins; Risk | 2013 |
Systemic uptake, albumin and hemoglobin binding of [(14)C]2,3-butanedione administered by intratracheal instillation in male Harlan Sprague Dawley rats and oropharyngeal aspiration in male B6C3F1/N mice.
Topics: Animals; Arginine; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Diacetyl; Hemoglobins; Intubation, Intratracheal; Male; Mice; Protein Binding; Rats; Rats, Sprague-Dawley; Serum Albumin; Tandem Mass Spectrometry | 2015 |