nad has been researched along with alpha-chymotrypsin in 47 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 38 (80.85) | 18.7374 |
| 1990's | 9 (19.15) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ertingshausen, G; Grossman, SH; Mollo, E | 1 |
| Pfleiderer, G | 1 |
| Jeck, R; Jörnvall, H; Sch9attle, E; Woenckhaus, C | 1 |
| Constantinides, SM; Marangos, PJ | 1 |
| Steinberg, IZ | 1 |
| Benecky, M; Kafina, M; McFarland, JT; Schmidt, J; Watters, KL | 1 |
| Burzio, LO; Koide, SS; Riquelme, PT | 1 |
| Jeck, R; Jörnvall, H; Woenckhaus, C | 1 |
| Collier, RJ; DeLange, RJ; Drazin, RE; Williams, LC | 1 |
| Churchill, S; Fleischer, S; Maurer, A; McIntyre, JO | 1 |
| Wang, JH | 1 |
| Brunel, C; Cantau, B; Pudles, J | 1 |
| Kaffarnik, H; Meyer-Bertenrath, JG | 1 |
| Rogers, KS | 1 |
| Della Corte, E; Stirpe, F | 1 |
| Deal, WC; Yang, ST | 1 |
| Green, RW; McKay, RH | 1 |
| Cassen, T; Kearns, DR | 1 |
| Kirschner, K | 1 |
| Cantau, BN; Jaureguiberry, GJ; Pudles, J | 1 |
| Fenselau, A | 1 |
| Berezin, IV; Luzikov, VN; Saks, VA | 1 |
| Gutfreund, H | 1 |
| Fensleau, A | 1 |
| Luzikov, VN; Romashina, LV | 1 |
| Spatz, L; Strittmatter, P | 1 |
| Scott, MD; Sykes, BD | 1 |
| Battelli, MG; Lorenzoni, E; Stripe, F | 1 |
| Axén, R; Vretblad, P | 1 |
| Liljas, A; Rossman, MG | 1 |
| Jörnvall, H; Koberstein, R; Noack, K; Rasched, I; Sund, H; Witzemann, V | 1 |
| Foucault, G; Levilliers, J; Pudles, J; Traore, F | 1 |
| Gan, EV; Haberman, HF; Menon, IA | 1 |
| Degani, Y; Nyc, JF; Smith, EL; Veronese, FM | 1 |
| Kaiser, ET; Lawrence, DS | 1 |
| Kameshita, I; Matsuda, Z; Shizuta, Y; Taniguchi, T | 1 |
| Lechene, C; Mroz, EA | 1 |
| Bodo, JM; Foucault, G | 1 |
| Bailey, JM; Chen, S; Deng, PS; Swiderek, KM | 1 |
| Ballou, DP; Gassner, GT | 1 |
| Gomi, T; Itagaki, E; Mizuguchi, M; Suzuki, K | 1 |
| Barbieri, JT; Krueger, KM | 1 |
| de Kok, A; Fabisz-Kijowska, A; Kester, H; Obels, PP; Westphal, AH | 1 |
| Chavan, AJ; Haley, BE; Sankaran, B | 1 |
| Dryjanski, M; Kosley, LL; Pietruszko, R | 1 |
| Alvarez-Gonzalez, R; Mendoza-Alvarez, H | 1 |
| Blanke, SR; Collier, RJ; Lodaya, R; Slama, JT | 1 |
3 review(s) available for nad and alpha-chymotrypsin
| Article | Year |
|---|---|
Circular polarization of luminescence: biochemical and biophysical applications.
Topics: Acridines; Amino Acids; Antibodies; Antigen-Antibody Reactions; Binding Sites; Biopolymers; Chlorophyll; Chymotrypsin; Coloring Agents; Conalbumin; Dipeptides; Europium; Lasalocid; Luminescent Measurements; Models, Biological; Molecular Conformation; NAD; Optical Rotation; Oxidoreductases; Phosphorylases; Proteins; Spectrum Analysis; Terbium; Transferrin; Tryptophan | 1978 |
Transients and relaxation kinetics of enzyme reactions.
Topics: Alcohol Oxidoreductases; Animals; Aspartic Acid; Catalase; Chemical Phenomena; Chemistry, Physical; Chymotrypsin; Computers; Endopeptidases; Enzymes; Escherichia coli; Flavoproteins; Glutamate Dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases; Hemoglobins; Homoserine; Horses; Hot Temperature; Kinetics; L-Lactate Dehydrogenase; Liver; Macromolecular Substances; Mathematics; Models, Biological; Muramidase; Myoglobin; NAD; Pancreas; Papain; Peroxidases; Phosphoric Monoester Hydrolases; Phosphotransferases; Protein Binding; Protein Conformation; Ribonucleases; Spectrophotometry; Temperature | 1971 |
Nuclear magnetic resonance studies of the dynamic aspects of molecular structure and interaction in biological systems.
Topics: Aspartate Carbamoyltransferase; Aspirin; Chymotrypsin; Histidine; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Muramidase; NAD; Penicillin G; Peptides; Protein Binding; Protein Conformation; Protein Denaturation; Ribonucleases; Serum Albumin; Staphylococcus; Sulfonamides; Tryptophan; Valinomycin | 1972 |
44 other study(ies) available for nad and alpha-chymotrypsin
| Article | Year |
|---|---|
Simplified, totally enzymatic method for determination of serum triglycerides with a centrifugal analyzer.
Topics: Alcohol Oxidoreductases; Autoanalysis; Centrifugation; Chymotrypsin; Evaluation Studies as Topic; Humans; Hydrogen-Ion Concentration; Kinetics; Lipase; Methods; NAD; Quality Control; Rhizopus; Triglycerides | 1976 |
On the role of tryptophan residues in the mechanism of action of glyceraldehyde-3phosphate dehydrogenase as tested by specific modification.
Topics: Apoproteins; Benzyl Compounds; Binding Sites; Chromatography, Gel; Chymotrypsin; Dialysis; Electrophoresis, Disc; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; NAD; Nitro Compounds; Protein Binding; Saccharomyces cerevisiae; Sulfhydryl Compounds; Sulfonium Compounds; Trypsin; Tryptophan | 1975 |
Modification of alcohol dehydrogenases with two NAD-+-analogues containing reactive substituents on the functional side of the molecule.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Chromatography, Gel; Chymotrypsin; Horses; Liver; NAD; Peptides; Protein Binding; Yeasts | 1975 |
Effect of NAD on flounder muscle glyceraldehyde 3-phosphate dehydrogenase.
Topics: Adenosine Triphosphate; Animals; Chymotrypsin; Drug Stability; Fishes; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Protein Denaturation; Trypsin; Urea | 1975 |
Resonance Raman investigation of beta-(2-furyl)-acryloyl-glyceraldehyde-3-phosphate dehydrogenase.
Topics: Acylation; Binding Sites; Chemical Phenomena; Chemistry; Chymotrypsin; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Protein Conformation; Spectrum Analysis, Raman | 1978 |
ADP ribosylation of rat liver lysine-rich histone in vitro.
Topics: Adenosine Diphosphate Sugars; Amino Acids; Animals; Cell Nucleus; Chymotrypsin; Histones; Kinetics; Liver; Lysine; NAD; Nucleoside Diphosphate Sugars; Peptide Fragments; Rats | 1979 |
Affinity labelling of yeast and liver alcohol dehydrogenases with the NAD analogue 4-(3-bromoacetylpyridinio)butyldiphosphoadenosine.
Topics: Affinity Labels; Alcohol Oxidoreductases; Animals; Binding Sites; Chymotrypsin; Cysteine; Horses; Kinetics; Liver; NAD; Peptide Fragments; Saccharomyces cerevisiae | 1979 |
The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. III. The chymotryptic peptides, the peptides derived by cleavage at tryptophan residues, and the complete sequence of the protein.
Topics: Adenosine Diphosphate Sugars; Amino Acid Sequence; Chymotrypsin; Diphtheria Toxin; NAD; Nucleotidyltransferases; Peptide Elongation Factors; Peptide Fragments; Ribose; Tryptophan | 1979 |
Phospholipid protection against proteolysis of D-beta-hydroxybutyrate dehydrogenase, a lecithin-requiring enzyme.
Topics: Animals; Apoenzymes; Carboxypeptidases; Carboxypeptidases A; Cattle; Chymotrypsin; Endopeptidases; Hydroxybutyrate Dehydrogenase; Liposomes; Metalloendopeptidases; Mitochondria, Heart; NAD; Peptide Fragments; Peptide Hydrolases; Phosphatidylcholines; Phospholipids; Pronase; Thermolysin; Trypsin | 1985 |
Facilitated proton transfer in enzyme catalysis. It may have a crucial role in determining the efficiency and specificity of enzymes.
Topics: Alcohol Oxidoreductases; Anhydrides; Anilides; Carbon Dioxide; Carbonic Anhydrases; Catalysis; Chemical Phenomena; Chemistry; Chymotrypsin; Enzymes; Kinetics; NAD; Protons; Ribonucleases | 1968 |
[Studies on the oxidative fraction obtained by chymotrypsin hydrolysis of glyceraldehyde-3-phosphate dehydrogenase].
Topics: Animals; Arsenic; Binding Sites; Centrifugation, Density Gradient; Chromatography, Gel; Chymotrypsin; Esterases; Fluorescence; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Molecular Weight; Muscles; NAD; Phosphoric Monoester Hydrolases; Rabbits; Spectrum Analysis; Sulfhydryl Compounds; Ultracentrifugation | 1968 |
[The properties of new substrates for the determination of pancreas enzymes].
Topics: Aspergillus; Chymotrypsin; Dicarboxylic Acids; Esters; Fatty Acids; Fluoresceins; Hydrogen-Ion Concentration; Kidney; Kinetics; Lipase; NAD; Pancreas; Pancreatin; Rhizopus | 1968 |
Protein fluorescence and inactivation of glutamate dehydrogenases during treatment with silver.
Topics: Animals; Cattle; Chickens; Chymotrypsin; Cytochromes; Fluorescence; Glutamate Dehydrogenase; Liver; NAD; Ribonucleases; Silver; Sulfhydryl Compounds | 1969 |
The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O).
Topics: Animals; Chymotrypsin; Female; Hydrogen-Ion Concentration; Liver; Male; Methylene Blue; NAD; Nitrogen; Oxygen; Rats; Surface-Active Agents; Trypsin; Uric Acid; Xanthine Oxidase; Xanthines | 1969 |
Metabolic control and structure of glycolytic enzymes. VII. Destabilization and inactivation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine phosphates and chymotrypsin.
Topics: Adenine; Adenine Nucleotides; Adenosine Triphosphate; Chemical Phenomena; Chemistry; Chymotrypsin; Cyclic AMP; Drug Stability; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Magnesium; NAD; Nucleosides; Nucleotides; Saccharomyces; Temperature; Time Factors | 1969 |
The behavior of horse liver alcohol dehydrogenase in guanidine hydrochloride solutions.
Topics: Alcohol Oxidoreductases; Alkylation; Animals; Chemical Phenomena; Chemistry; Chymotrypsin; Computers; Diffusion; Edetic Acid; Ethanol; Guanidines; Horses; Kinetics; Liver; Mathematics; Mercaptoethanol; Molecular Weight; NAD; Protein Denaturation; Ultracentrifugation; Viscosity; Zinc | 1969 |
Phosphorescence and energy transfer in enzymes.
Topics: Alcohol Oxidoreductases; Amylases; Animals; Aspergillus; Bacillus subtilis; Carboxypeptidases; Cattle; Chymotrypsin; Cold Temperature; Energy Transfer; Enzymes; Luminescent Measurements; Methods; Muramidase; NAD; Pancreas; Papain; Pepsin A; Ribonucleases; Saccharomyces; Spectrum Analysis; Tryptophan; Tyrosine | 1969 |
[Structural flexibility and enzyme function].
Topics: Binding Sites; Catalysis; Chemical Phenomena; Chemistry; Chymotrypsin; Enzymes; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; L-Lactate Dehydrogenase; Muramidase; NAD; Pyruvate Kinase; Transferases | 1969 |
Studies on the oxidative fraction of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Influence of ligands on its obtention enzymic properties.
Topics: Animals; Chymotrypsin; Cyclic AMP; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Oxidation-Reduction; Rabbits; Spectrophotometry; Ultracentrifugation | 1970 |
Structure-function studies on glyceraldehyde-3-phosphate dehydrogenase. 3. Dependency of proteolysis on NAD+ concentration.
Topics: Animals; Carbon Isotopes; Chemical Phenomena; Chemistry; Chymotrypsin; Electrophoresis, Disc; Endopeptidases; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Peptide Hydrolases; Protein Binding; Rabbits; Trypsin | 1970 |
Comparative study of thermal degradation of electron transfer particle and reconstituted respiratory chain. Relation of electron transfer to reactivation of submitochondrial particles.
Topics: Animals; Cattle; Chymotrypsin; Cytochromes; Electron Transport; Electron Transport Complex IV; Ferricyanides; Hot Temperature; Mitochondria, Muscle; Myocardium; NAD; Oleic Acids; Oxidoreductases; Oxygen; Potassium; Zinc | 1970 |
Structure-function studies on glyceraldehyde 3-phosphate dehydrogenase. IV. Subunit interactions of the rabbit muscle and yeast enzymes.
Topics: Allosteric Regulation; Animals; Binding Sites; Carbon Isotopes; Chymotrypsin; Dialysis; Endopeptidases; Filtration; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; Models, Chemical; Muscles; NAD; Pronase; Protein Binding; Protein Conformation; Rabbits; Saccharomyces; Saccharomyces cerevisiae; Species Specificity; Structure-Activity Relationship; Trypsin | 1972 |
Studies on stabilization of the oxidative phosphorylation system. II. Electron transfer-dependent resistance of succinate oxidase and NADH oxidase systems of submitochondrial particles to proteinases and cobra venom phospholipase.
Topics: Animals; Cattle; Chymotrypsin; Electron Transport; In Vitro Techniques; Mitochondria, Muscle; Myocardium; NAD; Oxidative Phosphorylation; Oxidoreductases; Phospholipases; Snakes; Spectrophotometry; Succinate Dehydrogenase; Trypsin; Venoms; Zinc | 1972 |
A form of reduced nicotinamide adenine dinucleotide-cytochrome b 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment.
Topics: Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Cattle; Chemical Phenomena; Chemistry; Chromatography, DEAE-Cellulose; Chymotrypsin; Cytochrome Reductases; Deoxycholic Acid; Electrophoresis, Disc; Ferricyanides; Isoelectric Focusing; Kinetics; Lysosomes; Membranes; Microsomes, Liver; Molecular Weight; NAD; Oxidoreductases; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet; Surface-Active Agents | 1973 |
Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties.
Topics: Animals; Cattle; Chymotrypsin; Dithiothreitol; Electrophoresis, Disc; Kinetics; Milk; Multienzyme Complexes; NAD; Papain; Spectrophotometry, Ultraviolet; Subtilisins; Thioctic Acid; Time Factors; Xanthine Oxidase | 1973 |
The use of isocyanides for the immobilization of biological molecules.
Topics: Acrylamides; Adenosine Monophosphate; Biotin; Chromatography, Gel; Chymotrypsin; Cyanides; Esters; Humans; Hydrogen-Ion Concentration; Leucine; Methods; Molecular Weight; NAD; Penicillanic Acid; Penicillin G; Phenylalanine; Protein Binding; RNA; Serum Albumin; Temperature; Tyrosine | 1973 |
Letter: Recognition of structural domains in globular proteins.
Topics: Amino Acid Sequence; Chymotrypsin; L-Lactate Dehydrogenase; NAD; Protein Binding; Protein Conformation; Structure-Activity Relationship | 1974 |
Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues.
Topics: Adenosine Diphosphate; Amino Acid Sequence; Amino Acids; Animals; Benzyl Compounds; Binding Sites; Cattle; Chromatography, Gel; Chymotrypsin; Circular Dichroism; Dansyl Compounds; Glutamate Dehydrogenase; Guanine Nucleotides; Hydrogen-Ion Concentration; Kinetics; Liver; NAD; Oxidation-Reduction; Peptide Fragments; Phenols; Protein Binding; Protein Conformation; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds; Tryptophan; Ultracentrifugation | 1974 |
Structure-function relationship in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues.
Topics: Animals; Apoproteins; Arsenic; Benzenesulfonates; Binding Sites; Chemical Phenomena; Chemistry; Chymotrypsin; Esters; Fluorobenzenes; Glyceraldehyde; Glyceraldehyde-3-Phosphate Dehydrogenases; Hot Temperature; Hydrogen; Kinetics; Lysine; Muscles; NAD; Nitrobenzenes; Organophosphorus Compounds; Phosphoric Acids; Polymers; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Structure-Activity Relationship | 1974 |
Oxidation of NADH by melanin and melanoproteins.
Topics: Amino Acids; Animals; Catechol Oxidase; Cattle; Chymotrypsin; Dihydroxyphenylalanine; Kinetics; Melanins; Melanoma; Mice; Mice, Inbred Strains; NAD; Neoplasms, Experimental; Oxidation-Reduction; Pepsin A; Peptide Hydrolases; Peptides; Phosphoproteins; Plants; Serum Albumin, Bovine; Time Factors; Trypsin | 1974 |
Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. III. Isolation and sequences of peptides containing selectively labeled lysine and cysteine residues.
Topics: Amino Acid Sequence; Amino Acids; Aminopeptidases; Binding Sites; Borohydrides; Carbon Radioisotopes; Carboxypeptidases; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Paper; Chymotrypsin; Cysteine; Electrophoresis, Paper; Ethylmaleimide; Glutamate Dehydrogenase; Leucyl Aminopeptidase; Lysine; NAD; Neurospora; Neurospora crassa; Oxidation-Reduction; Papain; Peptide Fragments; Protein Binding; Pyridoxal Phosphate; Thermolysin; Trypsin | 1974 |
Chemical mutation of enzyme active sites.
Topics: Anaerobiosis; Binding Sites; Catalysis; Chemical Phenomena; Chemistry; Chymotrypsin; Enzymes; Flavins; Kinetics; NAD; Niacinamide; Oxidation-Reduction; Papain; Stereoisomerism; Toluene | 1984 |
Poly (ADP-Ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain.
Topics: Animals; Binding Sites; Borohydrides; Carbon Radioisotopes; Cattle; Cellulose; Chymotrypsin; DNA; Molecular Weight; NAD; NAD+ Nucleosidase; Papain; Peptide Fragments; Poly(ADP-ribose) Polymerases; Protein Binding; Thymus Gland; Tritium | 1984 |
An NADH-coupled assay for femtogram or nanogram quantities of chymotrypsin.
Topics: Animals; Chymotrypsin; Fluorometry; Microchemistry; NAD; Rats; Spectrophotometry, Ultraviolet; Tyrosine | 1983 |
[Comparative study on the chemical modification of sulfhydryl groups of glyceraldehyde-3-phosphate dehydrogenases from yeast and rabbit muscle. The relationship between structure and chemical reactivity].
Topics: Animals; Chemical Phenomena; Chemistry; Chymotrypsin; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Rabbits; Structure-Activity Relationship; Sulfhydryl Compounds; Sulfhydryl Reagents; Yeasts | 1982 |
A two-domain structure for the two subunits of NAD(P)H:quinone acceptor oxidoreductase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Chymotrypsin; Dicumarol; Endopeptidases; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrolysis; Metalloendopeptidases; Molecular Sequence Data; NAD; NAD(P)H Dehydrogenase (Quinone); NADP; Peptide Fragments; Phenindione; Rats; Trypsin; Vitamin K | 1994 |
Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain.
Topics: Animals; Cattle; Chymotrypsin; Flavin Mononucleotide; Iron-Sulfur Proteins; Kinetics; Mathematics; Models, Theoretical; NAD; Oxidation-Reduction; Oxidoreductases; Pancreas; Spectrophotometry; Xanthine Oxidase | 1995 |
Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1.
Topics: Amino Acid Sequence; Binding Sites; Chymotrypsin; Lysine; Mixed Function Oxygenases; Molecular Sequence Data; NAD; Pseudomonas putida; Pyridoxal Phosphate; Trinitrobenzenesulfonic Acid | 1995 |
Molecular characterization of the in vitro activation of pertussis toxin by ATP.
Topics: Adenosine Diphosphate Ribose; Adenosine Triphosphate; Biotransformation; Blotting, Western; Chromatography, Gel; Chymotrypsin; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; GTP-Binding Proteins; Kinetics; Macromolecular Substances; NAD; Peptide Mapping; Pertussis Toxin; Phosphorus Radioisotopes; Recombinant Proteins; Trypsin; Virulence Factors, Bordetella | 1993 |
The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex.
Topics: Amino Acid Sequence; Azotobacter vinelandii; Binding Sites; Chymotrypsin; Dihydrolipoamide Dehydrogenase; Escherichia coli; Exonucleases; Ketoglutarate Dehydrogenase Complex; Kinetics; Molecular Sequence Data; Mutagenesis; NAD; Protein Binding; Protein Conformation; Pyruvate Dehydrogenase Complex; Recombinant Fusion Proteins; Spectrophotometry | 1995 |
Identification of adenine binding domain peptides of the NADP+ active site within porcine heart NADP(+)-dependent isocitrate dehydrogenase.
Topics: Adenine; Affinity Labels; Amino Acid Sequence; Animals; Azides; Binding Sites; Chromatography, Affinity; Chromatography, High Pressure Liquid; Chymotrypsin; Isocitrate Dehydrogenase; Mitochondria, Heart; Molecular Sequence Data; NAD; NADP; Peptide Mapping; Peptides; Photolysis; Swine; Trypsin | 1996 |
N-tosyl-L-phenylalanine chloromethyl ketone, a serine protease inhibitor, identifies glutamate 398 at the coenzyme-binding site of human aldehyde dehydrogenase. Evidence for a second "naked anion" at the active site.
Topics: Aldehyde Dehydrogenase; Amino Acid Sequence; Binding Sites; Chymotrypsin; Cytoplasm; Glutamic Acid; Humans; Isoenzymes; Kinetics; Mitochondria; Molecular Sequence Data; NAD; Peptide Fragments; Peptide Mapping; Serine Proteinase Inhibitors; Substrate Specificity; Tosylphenylalanyl Chloromethyl Ketone; Trypsin | 1998 |
Biochemical characterization of mono(ADP-ribosyl)ated poly(ADP-ribose) polymerase.
Topics: Adenosine Diphosphate Ribose; ADP Ribose Transferases; Animals; Catalysis; Cattle; Chromatin; Chymotrypsin; Hydrolysis; Liver; NAD; Papain; Poly(ADP-ribose) Polymerases; Rats; Substrate Specificity | 1999 |
Photoaffinity labeling of diphtheria toxin fragment A with 8-azidoadenosyl nicotinamide adenine dinucleotide.
Topics: Amino Acid Sequence; Azides; Binding Sites; Catalysis; Chromatography, Affinity; Chromatography, High Pressure Liquid; Chymotrypsin; Diphtheria Toxin; Hydrolysis; Metalloendopeptidases; Models, Molecular; Molecular Sequence Data; NAD; Peptide Fragments; Photoaffinity Labels; Serine Endopeptidases; Substrate Specificity | 1999 |