This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Libenson, L. Articles by Jena, M. Search for Related Content PubMed PubMed Citation Articles by Libenson, L. Articles by Jena, M.

Uptake of Glutathione by Serum Albumin of Normal and Tumor-bearing Mice¹

Division of Medical Education and Research, The Western Pennsylvania Hospital, Pittsburgh, Pennsylvania 15224

Single doses of ³⁵S-labeled reduced glutathione (GSH) were administered intraperitoneally to groups of normal and tumor-bearing mice, and radioactivity was determined in the protein and non-protein fractions of blood serum. The results show that GSH is taken up rapidly by the albumin fraction of serum protein.

Experiments in vitro showed that both mouse and human serum albumin react with GSH in aerobic mixtures at pH values near neutrality and yield a mixed disulfide through oxidation of their thiol groups. Unlike the intermediate mixed disulfides produced in the reduction of albumin disulfide groups by GSH at low pH under anaerobic conditions, this mixed disulfide is relatively stable in slightly alkaline solution and exhibits no apparent change in the tertiary structure of the albumin moiety. It releases free GSH on incubation with tumor and liver homogenates.

The findings indicate that albumin and GSH may interact by two different mechanisms which are operative depending on the pH and on the presence or absence of free oxygen in the medium. The possible physiologic significance of these mechanisms is discussed.

¹ This investigation was aided by Research Grant No. Ca-06345 from the NIH, USPHS.

Received 8/16/66. Accepted 3/ 6/67.