| Literature DB >> 3277619 |
A Llobell1, A Lopez-Ruiz, J Peinado, J Lopez-Barea.
Abstract
Yeast glucose-6-phosphate dehydrogenase was inhibited by low NADPH concentrations in cell-free extracts, and de-inhibited by GSSG; extensive dialysis of the crude extract did not diminish the GSSG effect. Immunoprecipitation of glutathione reductase abolished the de-inhibition of glucose-6-phosphate dehydrogenase by GSSG. Purified glucose-6-phosphate dehydrogenase was inhibited by NADPH but not de-inhibited by GSSG, and upon addition of pure glutathione reductase GSSG completely de-inhibited the glucose-6-phosphate dehydrogenase.Entities:
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Year: 1988 PMID: 3277619 PMCID: PMC1148696 DOI: 10.1042/bj2490293
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857