PMID: 2493824Feb 1, 1989Paper

Isolation of estrophilic fractions of hydroxysteroid dehydrogenase from rabbit liver

Biulleten' eksperimental'noĭ biologii i meditsiny
A N Smirnov, T A Shchelkunova

Abstract

Estrophilic forms of rabbit liver cytosolic hydroxysteroid-dehydrogenase (HSD) were obtained as a highly purified preparations by means of fractionation with ammonium sulfate, gel-filtration, ion-exchange chromatography on DEAE-Sephadex A-50, affinity chromatography on estradiol-Sepharose and ion-exchange chromatography on DEAE-Toyopearl 650M. The protein express 4 different kinds of NADP-dependent activities: 3 alpha, 3 beta- and 17 beta-HSD activities with androgens and 20 alpha-HSD with progesterone as substrates. Revealed multiplicity of HSD enzymatic activity is demonstrated here for the first time. 17 beta-HSD activity of the protein preparations with estradiol is extremely low. Absence of a real metabolic activity of the protein with a ligand interacting with it rather intensively suggests that the isolated HSD forms can act not only as an enzyme, but also as a buffer-reserving mechanism for some steroids.

References

May 1, 1977·Molecular and Cellular Endocrinology·E R de KloetG H Mulder
Nov 15, 1973·Journal of Molecular Biology·U K Laemmli, M Favre
Feb 27, 1980·Biochemical and Biophysical Research Communications·J R Smalley, E F Sarcione
Feb 29, 1984·Biochemical and Biophysical Research Communications·G Mendoza-HernándezJ C Díaz-Zagoya
Jul 1, 1984·Journal of Steroid Biochemistry·M F Ruh, D O Toft

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