Characterization of the androgen-dependent 22Kdalton glycoprotein from rat ventral prostate.
Oxidation by molecular oxygen converted the 22Kdalton glycoprotein from rat ventral prostate into a 34K species and this reaction could be reversed by thiol reducing reagent. Measurement of the level of the 22Kdalton glycoprotein in prostatic cytosol by the radial immunodiffusion technique showed that changes in the 22Kdalton glycoprotein concentration in response to androgen withdrawal and replacement were slow in comparison to androgen regulated levels of mRNA coding for the protein. (3) Charcoal absorption steroid binding assays of the 22Kdalton glycoprotein revealed that the protein did not bind testosterone, estradiol, progesterone or corticosterone. These results indicate that the 22Kdalton glycoprotein is metabolically stable, not steroid-binding, and exists as an oligomer through disulfide crosslinking.
Wang
T Y
TY
Chamberlin
L L
LL
Xu
Y H
YH
D000818:Animals; D006023:Glycoproteins / Q000302:isolation & purification* / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D009919:Orchiectomy; D010084:Oxidation-Reduction; D011467:Prostate / Q000187:drug effects / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains; D013256:Steroids / Q000378:metabolism; D013739:Testosterone / Q000494:pharmacology
D006023:Glycoproteins; D013256:Steroids; D013739:Testosterone