Glutathione biosynthesis in human erythrocytes

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Glutathione synthesis in human erythrocytes. II. Purification and properties of the enzymes of glutathione biosynthesis.

The two enzymes required to synthesize glutathione de novo have been purified from human erythrocytes. Glutamylcysteine synthetase was purified 4300-fold and was approximately 80% pure based on polyacrylamide gel electrophoresis. The purified enzyme catalyzes the formation of 30.5 mumoles of gamma-glutamyl-cysteine per mg of protein per hr and is inhibited by sulfhydryl inhibitors. Glutathione ...

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Transport of glutathione-conjugates in human erythrocytes.

The last step of detoxification of both endogenous and environmental toxicants is typically a conjugation that produces a bulky hydrophilic molecule. The excretion of such conjugates out of cells is of sufficient biological importance to have led to the evolution of ATP-driven export pumps for this purpose. The substrate specificity of such transporters is broad, and in some cases it has been s...

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Porphyrin Biosynthesis in Erythrocytes

The porphyrinogens are colorless, reduced porphyrins containing 6 extra atoms of hydrogen. They have been reported to occur in biological materials by Fischer, who isolated COPRO’gen’ from the feces of his porphyria patient Petry (l), and by Watson, Schwartz, and coworkers, who showed that COPRO’gen was present in the urine of some of their patients with various porphyrias (2). Suspicions that ...

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Transport accounts for glutathione turnover in human erythrocytes.

Human erythrocytes were incubated with 3H-glycine to label the glutathione pool. These cells were then used to determine the rate of oxidized glutathione (GSSG) transport out of erythrocytes. For 6 normal individuals, the mean transport rate was 6.7 nmole GSSG/hr/ml red cells. This transport rate would suggest a half-life of 4.7 days for the erythrocytic glutathione, which is in close agreemwnt...

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Glutathione transport by inside-out vesicles from human erythrocytes.

Purified inside-out vesicles from human erythrocytes were used to investigate the active transport of oxidized glutathione (GSSG). Incubation of vesicles and GSSG in the presence of ATP resulted in the transport of GSSG into the vesicles. When vesicles were incubated with reduced glutathione (GSH), no transport was observed. At GSSG concentrations of less than 5 mM, transport was linear up to 4...

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ژورنال

عنوان ژورنال: Journal of Clinical Investigation

سال: 1971

ISSN: 0021-9738

DOI: 10.1172/jci106519