| Literature DB >> 14333550 |
Abstract
1. Measurements of kinetic constants for a purified preparation of human-placenta oestradiol dehydrogenase have been made. 2. These constants have been compared with similar measurements made on crude ammonium sulphate precipitates of human-placenta homogenates. The comparison indicates that nearly half of the observed nicotinamide nucleotide-transhydrogenation activity in the crude preparations is due to a specific oestrogen-dependent transhydrogenase. 3. The remainder of the observed activity results from a substrate-mediated transhydrogenation catalysed by the oestradiol-dehydrogenase activities present in the preparation.Entities:
Keywords: BIOCHEMISTRY; CATALYSIS; ESTRADIOL; ESTRONE; EXPERIMENTAL LAB STUDY; KINETICS; NAD; NADP; OXIDOREDUCTASES; PLACENTA; SPECTROPHOTOMETRY
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Year: 1965 PMID: 14333550 PMCID: PMC1215188 DOI: 10.1042/bj0950150
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857