Binding of steroid hormones and anabolic agents to bovine sex-hormone binding globulin.
Binding of some selected steroids and anabolic agents to bovine sex-hormone binding globulin (SHBG) was investigated. SHBG binding affinities, relative to the reference hormone 5 alpha-dihydrotestosterone, were estimated for the compounds. The results demonstrate that binding of steroid hormones to SHBG is facilitated by the 17 beta-hydroxyl group, possibly involving hydrogen binding, and by the methyl group at C-19 of the steroid moiety. Structural modifications at C-17 of a steroid molecule involving esterification, epimerization or reduction of the 17 beta-hydroxyl group, or introduction of a bulky 17 alpha group have the effect of decreasing the SHBG binding affinity of the steroid molecule.
D000735:Androstenedione / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D013196:Dihydrotestosterone / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism; D012738:Sex Hormone-Binding Globulin / Q000378:metabolism*; D013256:Steroids / Q000378:metabolism*; D013739:Testosterone / Q000378:metabolism; D014204:Trenbolone Acetate / Q000378:metabolism; D015029:Zeranol / Q000378:metabolism
D012738:Sex Hormone-Binding Globulin; D013256:Steroids; D013196:Dihydrotestosterone; D013739:Testosterone; D000735:Androstenedione; D004958:Estradiol; D015029:Zeranol; D014204:Trenbolone Acetate