| Literature DB >> 7248317 |
Abstract
The cytoplasmic NADPH-dependent prostaglandin D2 11-keto reductase from rabbit liver was purified by a series of chromatographic procedures including isoelectric focusing. The enzyme catalyzed the conversion of prostaglandin D2 to prostaglandin F2 alpha and had a pH optimum of 7.0-7.5, and an isoelectric point of 5.8. The molecular weight was estimated to be 66 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymic activity was time and concentration dependent and required NADPH as cofactor.Entities:
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Year: 1981 PMID: 7248317 DOI: 10.1016/0005-2744(81)90281-3
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002