[Isolation of estrophilic fractions of hydroxysteroid dehydrogenase from rabbit liver].
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.
Smirnov
A N
AN
Shchelkunova
T A
TA
D000327:Adsorption; D000818:Animals; D002352:Carrier Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D004958:Estradiol / Q000378:metabolism*; D006913:Hydroxysteroid Dehydrogenases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008297:Male; D008722:Methods; D011817:Rabbits; D012738:Sex Hormone-Binding Globulin; D012995:Solubility; D014316:Tritium
D002352:Carrier Proteins; D012738:Sex Hormone-Binding Globulin; D014316:Tritium; D004958:Estradiol; D006913:Hydroxysteroid Dehydrogenases
Vydelenie éstrofil'nykh fraktsiĭ oksisteroiddegidrogenazy pecheni krolika.