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A possible functional relationship between microsomal aromatic aldehyde-ketone reductase and hexose-6-phosphate dehydrogenase.

作者信息

Sawada H, Hayashibara M, Hara A, Nakayama T

出版信息

J Biochem. 1980 Mar;87(3):985-8. doi: 10.1093/oxfordjournals.jbchem.a132829.

DOI:10.1093/oxfordjournals.jbchem.a132829
PMID:6993453
Abstract

Aromatic ketone reductase activity of microsomes showed a unique cofactor requirement: Addition of NADP and glucose-6-phosphate was as effective as that of an artificial NADPH generating system, whereas NADPH alone served as a cofactor less efficiently. Microsomal aromatic ketone reductase, purified partially from guinea pig liver microsomes after solubilization with Triton X-100, reduced 5 beta-dihydrotestosterone, aromatic aldehydes, and ketones with NADPH as a cofactor. However, addition of hexose-6-phosphate dehydrogenase, purified from the same source, as an NADPH generator produced about 2 times higher activity than that of yeast glucose-6-phosphate dehydrogenase or NADPH alone.

摘要

相似文献

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