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Purification and properties of polyol dehydrogenase from Cephalosporium chrysogenus.

作者信息

Birken S, Pisano M A

出版信息

J Bacteriol. 1976 Jan;125(1):225-32. doi: 10.1128/jb.125.1.225-232.1976.

DOI:10.1128/jb.125.1.225-232.1976
PMID:1374
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC233356/
Abstract

A polyol dehydrogenase of broad specificity was purified 178-fold from extracts of the filamentous fungus Cephalosporium chrysogenum. The enzyme was found to act as an oxido-reductase in two substrate-coenzyme systems: D-sorbitol (or xylitol)-nicotinamide-adenine dinucleotide (NAD) and D-mannitol-nicotinamide adenine dinucleotide phosphate (NADP). The dehydrogenase was composed of five isozymes, which, as a mixture, exhibited these properties: Km to D-sorbitol and D-mannitol, 7.15 to 10(-2) M; PH optimum, 9 to 10; molecular weight, 300,000 subunit weight, 29,000; PI, 5.8 to 7.5. The NADP-linked activity was labile to treatment with heat or ethylenediaminetetraacetic acid. Mixed substrate assays support the hypothesis that both NAD-, and NADP-linked activities are associated with isozymes of a single dehydrogenase.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/035e/233356/18dbf7bd83e2/jbacter00320-0240-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/035e/233356/18dbf7bd83e2/jbacter00320-0240-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/035e/233356/18dbf7bd83e2/jbacter00320-0240-a.jpg

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