Comparison of the multiple forms of the soluble 3(17) alpha-hydroxysteroid dehydrogenases of female rabbit kidney and liver.
Multiple forms of the soluble 17 alpha-hydroxysteroid dehydrogenases of female rabbit liver and kidney having similar purification characteristics and isoelectric points were compared with regard to their relative rates of oxidation and reduction of estrogen and androgen substrates, their kinetic parameters and their primary structures. All of the enzyme forms exhibited both 3 alpha- and 17 alpha-enzyme activity toward androgen substrates and the oxidation of the 17 alpha-hydroxysteroid epitestosterone was competitively inhibited by the 3 alpha-hydroxysteroid androsterone. The most basic enzyme forms from liver and kidney had similar relative activities toward estrogen and androgen substrates in the oxidative direction but differed in their activities in the reductive direction. Major differences in the peptide maps of these enzymes were observed. The less basic enzyme forms from the two tissues had similar activities toward estrogen substrates but differed considerably in their relative activities toward androgens. Only minor differences were observed in the peptide maps of these enzymes.
D000728:Androgens / Q000378:metabolism; D000738:Androsterone / Q000378:metabolism; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004845:Epitestosterone / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism; D004967:Estrogens / Q000378:metabolism; D005260:Female; D006913:Hydroxysteroid Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits
D000728:Androgens; D004967:Estrogens; D010446:Peptide Fragments; D004845:Epitestosterone; D004958:Estradiol; D000738:Androsterone; D006913:Hydroxysteroid Dehydrogenases; C035507:3(17)-hydroxysteroid dehydrogenase