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Purification and some properties of sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae

✍ Scribed by Joseph R. Merkel; Martin Straume; Susan A. Sajer; Robert L. Hopfer

Publisher: Elsevier Science
Year: 1982
Tongue: English
Weight: 810 KB
Volume: 122
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(82)90268-8

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✦ Synopsis

An NAD-dependent glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ oxidoreductase, EC 1.1.1.8) has been isolated and purified from Saccharomyces cerevisiae by affinity and exclusion chromatography. The enzyme was purified 5 1 OO-fold to a specific activity of 158. It has a molecular weight of approximately 31,000, a pH optimum between 6.8 and 7.2, and is sensitive to high-ionic-strength salt solutions. The enzyme is most strongly inhibited by phosphate and chloride ions.

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