Page last updated: 2024-08-16

iodoacetic acid and arginine

iodoacetic acid has been researched along with arginine in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19902 (25.00)18.7374
1990's5 (62.50)18.2507
2000's1 (12.50)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Asryants, RA; Kuzminskaya, EV; Nagradova, NK1
Davis, JP; Van Etten, RL; Zhang, ZY1
Reizer, J; Saier, MH1
Bittar, EE; Chiang, L; Sharpe, T1
Focia, P; Kanaani, J; Maltby, D; Wang, CC1
Curtis, MA; Rangarajan, M; Smith, SJ; U, S1
Govil, G; Patel, AB; Phadke, RS; Srivastava, S1
Kaback, HR; Sahin-Tóth, M1

Other Studies

8 other study(ies) available for iodoacetic acid and arginine

ArticleYear
Rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase: half-of-the-sites reactivity of the enzyme modified at arginine residues.
    Biochemical and biophysical research communications, 1992, Sep-16, Volume: 187, Issue:2

    Topics: Animals; Apoenzymes; Arginine; Binding Sites; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrolysis; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Macromolecular Substances; Muscles; NAD; Nitrophenols; Protein Conformation; Rabbits; Structure-Activity Relationship

1992
Covalent modification and active site-directed inactivation of a low molecular weight phosphotyrosyl protein phosphatase.
    Biochemistry, 1992, Feb-18, Volume: 31, Issue:6

    Topics: Animals; Arginine; Arsenicals; Binding Sites; Binding, Competitive; Cattle; Cyclohexanones; Cysteine; Epoxy Compounds; Glutathione; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Molecular Weight; Phenylglyoxal; Protein Tyrosine Phosphatases

1992
Mechanism and regulation of phosphate transport in Streptococcus pyogenes.
    Journal of bacteriology, 1987, Volume: 169, Issue:1

    Topics: Adenosine Triphosphate; Arginine; Arsenates; Biological Transport, Active; Glucose; Glycolysis; Iodoacetates; Iodoacetic Acid; Kinetics; Phosphates; Sodium Fluoride; Streptococcus pyogenes

1987
Some quantitative aspects of myoplasmic ATPMg and total internal ATP and ArP levels in resting barnacle muscle fibres.
    Comparative biochemistry and physiology. B, Comparative biochemistry, 1983, Volume: 75, Issue:1

    Topics: Adenosine Triphosphate; Animals; Arginine; Arginine Kinase; Deoxyglucose; Diethyl Pyrocarbonate; Firefly Luciferin; Iodoacetates; Iodoacetic Acid; Luciferases; Luminescent Measurements; Methods; Mitochondrial ADP, ATP Translocases; Muscles; Organophosphorus Compounds; Thoracica

1983
Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2',3'-dialdehyde affinity labeling.
    Biochemistry, 1995, Nov-21, Volume: 34, Issue:46

    Topics: Affinity Labels; Amino Acid Sequence; Animals; Arginine; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Iodoacetates; Iodoacetic Acid; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Phosphoribosyl Pyrophosphate; Schistosoma mansoni; Sequence Analysis; Trypsin

1995
Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor.
    The Biochemical journal, 1997, May-01, Volume: 323 ( Pt 3)

    Topics: Adhesins, Bacterial; Amino Acid Sequence; Arginine; Bacterial Proteins; Binding Sites; Cysteine Endopeptidases; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Evolution, Molecular; Gingipain Cysteine Endopeptidases; Hemagglutinins; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Leucine; Molecular Sequence Data; Molecular Weight; Porphyromonas gingivalis; Protease Inhibitors; Substrate Specificity; Virulence

1997
Arginine acts as a protective and reversal agent against glycolytic inhibitors in spermatozoa.
    Physiological chemistry and physics and medical NMR, 1999, Volume: 31, Issue:1

    Topics: Animals; Antispermatogenic Agents; Arginine; Enzyme Inhibitors; Glucose; Glycolysis; Goats; In Vitro Techniques; Iodoacetamide; Iodoacetic Acid; Lactic Acid; Magnetic Resonance Spectroscopy; Male; Spermatozoa

1999
Functional conservation in the putative substrate binding site of the sucrose permease from Escherichia coli.
    Biochemistry, 2000, May-23, Volume: 39, Issue:20

    Topics: Alkylation; Arginine; Aspartic Acid; Binding Sites; Biological Transport, Active; Chromatography, Affinity; Conserved Sequence; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Iodoacetic Acid; Membrane Transport Proteins; Mutagenesis, Site-Directed; Serine; Substrate Specificity; Sucrose

2000