TRANSHYDROGENATION IN THE HUMAN PLACENTA
Copyright policy )TRANSHYDROGENATION IN THE HUMAN PLACENTA
ABSTRACT Human placental 17β-oestradiol dehydrogenase exists in two electrophoretic forms which are either isozymes or components of a monomerpolymer system. Both forms utilize NAD+ and NADP+ as cofactor and 17β-oestradiol-3-sulfate and testosterone as substrate. Using a method developed to detect transhydrogenase activity on starch gel after electrophoresis, both forms were shown to mediate transhydrogenation but transhydrogenase:dehydrogenase activity ratios of the two forms were different. No oestrogen-sensitive transhydrogenase distinct from 17β-oestradiol dehydrogenase was observed on electrophoresis of placental crude supernatant and purified preparations at several pH values.
Electrophoresis, Estradiol, Placenta, Humans, Female, In Vitro Techniques, NAD, Oxidoreductases, NADP
Electrophoresis, Estradiol, Placenta, Humans, Female, In Vitro Techniques, NAD, Oxidoreductases, NADP
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