Abstract
An androgen binding activity with characteristics similar to ABP is present in a particulate fraction (105,000 g pellet) obtained by differential centrifugation of seminiferous tubules, impure Sertoli cells and impure germ cells homogenates. Purification of germ cells through albumin gradients, results in almost a complete loss of androgen binding activity in the purified germ cell suspensions. Furthermore, Sertoli cell enriched testes from 22-, 32- and 40-day old rats showed increases in particulate androgen binding, when compared to matched controls, parallel to increments in the activity of a Sertoli cell marker enzyme (β-glucuronidase). These results suggest that particulate androgen binding activity is only present in Sertoli cells and this protein may play a role in the compartmentalization of androgens in the testis.
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