Abstract
Androgen binding protein (ABP) was isolated from rat testes and epididymides by affinity chromatography. Rat ABP is a glycoprotein with a native molecular weight of 85,000 daltons. This protein is comprised of 45,000 and 41.000 dalton components (rABP h and rABP l in a ratio of 3:1. rABP h and rABP l have similar polypcptide chains with identical binding sites. Part of the difference in these protomers is due to their carbohydrate compositions. A major portion of rABP is secreted by Sertoli cells into the seminiferous tubular lumen and from there, it is transported to the epididymis. The remainder is secreted into the blood. Evidence is reviewed supporting the postulate that most of rABP that enters the blood is released from the base of the Sertoli cells. A kinetic analysis of the disappearance of rABP from blood following removal of the testes plus the epididymides versus removal of only the testes suggests that the epididymides can release ABP into the blood during androgen deprivation. A study of hypophysectomized rats supports this postulate. Results are also presented which suggest that progestins, in addition to testosterone and FSH. stimulate ABP release into the blood.
Published Version
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