Modulation of the hydrophobicity of glutamine synthetase by mixed‐function oxidation
- 1 July 1988
- journal article
- research article
- Published by Wiley in The FASEB Journal
- Vol. 2 (10) , 2591-2595
- https://doi.org/10.1096/fasebj.2.10.2898411
Abstract
Oxidative modification of Escherichia coli glutamine synthetase renders the enzyme susceptible to proteolytic degradation by a specific protease purified from the bacterium; native enzyme is not a su...Keywords
This publication has 13 references indexed in Scilit:
- Purification of neutral lens endopeptidase: close similarity to a neutral proteinase in pituitary.Proceedings of the National Academy of Sciences, 1985
- Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase.Journal of Biological Chemistry, 1985
- Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscleBiochemical Journal, 1985
- Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases.Journal of Biological Chemistry, 1985
- Oxidative inactivation of glutamine synthetase subunits.Proceedings of the National Academy of Sciences, 1984
- Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue.Journal of Biological Chemistry, 1983
- Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system.Journal of Biological Chemistry, 1983
- Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis.Proceedings of the National Academy of Sciences, 1981
- Cation‐Sensitive Neutral Endopeptidase: Isolation and Specificity of the Bovine Pituitary EnzymeJournal of Neurochemistry, 1980
- A correlation between turnover rates and lipophilic affinities of soluble rat liver proteinsBiochemical and Biophysical Research Communications, 1976