Inactivation of mitochondrial carbamoyl phosphate synthetase induced by ascorbate, oxygen, and Fe3+ in the presence of acetylglutamate: Protection by ATP and HCO−3 and lack of inactivation of ornithine transcarbamylase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference45 articles.
1. The Importance of Both Synthesis and Degradation in the Control of Arginase Levels in Rat Liver
2. Control of Proteolysis
3. Regulation of Mitochondrial Protein Concentration: A Plausible Model Which May Permit Assessing Protein Turnover
4. EXTRALYSOSOMAL PROTEIN DEGRADATION
Cited by 8 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Arginine Biosynthesis in Thermotoga maritima : Characterization of the Arginine-Sensitive N -Acetyl- l -Glutamate Kinase;Journal of Bacteriology;2004-09-15
2. Oxidative inactivation of carbamoyl phosphate synthetase (ammonia). Mechanism and sites of oxidation, degradation of the oxidized enzyme, and inactivation by glycerol, EDTA, and thiol protecting agents.;Journal of Biological Chemistry;1992-03
3. Ascorbic acid and oxidative inactivation of proteins;The American Journal of Clinical Nutrition;1991-12-01
4. Influence of anions on the activation of carbamoyl phosphate synthetase (ammonia) by acetylglutamate: Implications for the activation of the enzyme in the mitochondria;Archives of Biochemistry and Biophysics;1991-08
5. Levels of carbamoyl phosphate synthetase I in livers of young and old rats assessed by activity and immunoassays and by electron microscopic immunogold procedures.;Journal of Histochemistry & Cytochemistry;1990-03
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