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Glutathione status in constituted physiological fluids containing albumin
U M Joshi1, K S Rao, H M Mehendale
1Department of Pharmacology and Toxicology, University of Mississippi Medical Center, Jackson 39216.
The International Journal of Biochemistry
|January 1, 1987
Summary
Bovine serum albumin (BSA) accelerates glutathione (GSH) oxidation in media, primarily through metal ion-dependent reactions. Catalase and alkaline pH enhance this process, suggesting a specific oxidative mechanism.
Area of Science:
- Biochemistry
- Oxidative Stress
- Protein-Ligand Interactions
Background:
- Glutathione (GSH) is a critical endogenous antioxidant.
- Bovine serum albumin (BSA) is a common protein supplement in biological media.
- The interaction between GSH and BSA can influence GSH stability and redox status.
Purpose of the Study:
- To investigate the mechanism of GSH and cysteine disappearance in BSA-supplemented media.
- To identify factors influencing BSA-mediated GSH oxidation.
- To elucidate the role of metal ions and pH in this oxidative process.
Main Methods:
- Incubation of GSH and cysteine with BSA in various media conditions.
- Analysis of GSH, cysteine, and GSSG concentrations using chromatographic methods.
- Assessment of the effects of oxygen levels, scavengers (catalase, SOD), metal ions, and pH on GSH oxidation.
Main Results:
- BSA rapidly decreased GSH and cysteine levels, primarily through oxidation to GSSG.
- GSH oxidation was dependent on oxygen, metal ions, and alkaline pH (above 7.4).
- Catalase significantly reduced BSA-mediated GSH oxidation, while other scavengers had no effect.
Conclusions:
- BSA promotes GSH oxidation via a mechanism involving mixed disulfide formation and subsequent reduction.
- Metal ions and alkaline pH are crucial for BSA-mediated GSH oxidation.
- Catalase plays a role in mitigating this oxidative process, suggesting a peroxide-dependent pathway.