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Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation.
Analysis shows that the inactivation of the activated enzyme was due to oxygen but unrelated to either the presence of substrate, enzyme turnover or accumulation of inhibitor produced during assay, and loss of activity during assay in the absence of protein-A was shown to be a first order decay process.
Purification and some properties of rat liver cysteine oxidase (cysteine dioxygenase).
Cysteine oxidase (cysteine dioxygenase, EC 1.13.20) was purified approximately 1000-fold from rat liver as an inactive form, which was activated by anaerobic preincubation with L-cysteined.
The effect of pyrazines on the metabolism of tryptophan and nicotinamide adenine dinucleotide in the rat. Evidence of the formation of a potent inhibitor of aminocarboxy-muconate-semialdehyde
Results suggest that the glutarate pathway of L-tryptophan was strongly inhibited by the inhibitor produced after the administration of pyrazinoic acid and pyrazinamide, which exhibited a significant inhibition of the nuclear enzyme poly(ADP-ribose) synthetase in rat liver.
Induction and activation of cysteine oxidase of rat liver. II. The measurement of cysteine metabolism in vivo and the activation of in vivo activity of cysteine oxidase.
The facts presented in this paper strongly suggest that the degradation of L -cysteine is metabolized mainly through cysteine sulfinate, and therefore the incorporation of 14 CO 2 into expired CO 2 from L -[U- 14 C]cy Steine is a reflection of the in vivo activity of cysteines oxidase.
Induction and activation of cysteine oxidase of rat liver: I. The effects of cysteine, hydrocortisone and nicotinamide injection on hepatic cysteine oxidase and tyrosine transaminase activities of
Abstract 1. 1. The greatest increase in hepatic cysteine oxidase activity was observed in intact rats which received cysteine, but the increase in tyrosine transaminase activity mediated by cysteine
Cysteine metabolism in vivo of vitamin B6-deficient rats.
The in vivo metabolic distribution of L-cysteine calculated showed that the remarkable lesion in taurine pathway occurred in pyridoxine deficient rats, and when non-physiological dose of L the catabolism in deficient rats was markedly increased in either pyruvate or taurusine pathway.
Interaction with mitochondrial membranes of a synthetic peptide with a sequence common to extra peptides of mitochondrial precursor proteins.
The results suggest the existence of a common protein receptor on mitochondrial membranes that facilitates entrance of a group of mitochondrial precursor proteins, including pre-ATPase inhibitor.
Two components of cysteine oxidase in rat liver.
Abstract Purified cysteine oxidase in rat liver is composed of two distinct proteins. These proteins are able to be fractionated by DEAE-cellulose column chromatography. It appears that one of them
Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.
Observations suggest that liver Bprotein is D-aspartate oxidase and E. coli B protein is L-as Partic acid oxidase, which is a substrate for quinolinic acid synthesis in a system composed of the B protein replacing activity of mammalian liver andE.