Compounds > hydroxylamine

hydroxylamine and 1,2-cyclohexanedione

hydroxylamine has been researched along with 1,2-cyclohexanedione in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's2 (50.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cummins, BJ; Dischinger, HC; Ullah, AH1
Berrocal, F; Carreras, J1
Bieth, JG; Davril, M; Duportail, G; Han, KK; Jung, ML; Lohez, M1
Antón, LC; Barrio, E; Gavilanes, F; Marqués, G; Ruiz, S; Sánchez, A; Vivanco, F1

Other Studies

4 other study(ies) available for hydroxylamine and 1,2-cyclohexanedione

ArticleYear
Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase.
    Biochemical and biophysical research communications, 1991, Jul-15, Volume: 178, Issue:1

    Topics: 6-Phytase; Amino Acids; Arginine; Aspergillus; Binding Sites; Chromatography, High Pressure Liquid; Cyclohexanones; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Kinetics; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Sequence Homology, Nucleic Acid; Substrate Specificity

1991
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.
    Comparative biochemistry and physiology. B, Comparative biochemistry, 1983, Volume: 76, Issue:1

    Topics: Animals; Arginine; Cyclohexanones; Diacetyl; Glyoxal; Hydroxylamine; Hydroxylamines; Muscles; Phenylglyoxal; Phosphoglycerate Mutase; Phosphoric Monoester Hydrolases; Phosphotransferases; Pyruvaldehyde; Rabbits

1983
Arginine modification in elastase. Effect on catalytic activity and conformation of the calcium-binding site.
    The Journal of biological chemistry, 1984, Mar-25, Volume: 259, Issue:6

    Topics: Animals; Arginine; Calcium; Cyclohexanones; Diacetyl; Hydroxylamine; Hydroxylamines; Kinetics; Pancreas; Pancreatic Elastase; Phenylglyoxal; Protein Conformation; Swine

1984
Arginine residues of the globular regions of human C1q involved in the interaction with immunoglobulin G.
    The Journal of biological chemistry, 1993, May-15, Volume: 268, Issue:14

    Topics: Amino Acid Sequence; Animals; Antigen-Antibody Complex; Arginine; Binding Sites, Antibody; Chromatography, High Pressure Liquid; Complement C1q; Cyclohexanones; Diethyl Pyrocarbonate; Histidine; Humans; Hydroxylamine; Hydroxylamines; Immunoglobulin G; Kinetics; Macromolecular Substances; Molecular Sequence Data; Peptide Fragments; Phenylglyoxal; Protein Conformation; Rabbits

1993