Beta glucuronidase-rich cytoplasmic particles in androgen-stimulated mouse kidney. A cytobiochemical study.

Androgens produced by stimulating mouse testis with gonadotropic hormones cause a rise in renal beta-glucuronidase but not an increase in acid or alkaline phosphatase. All subcellular components increase in beta-glucuronidase activity, with a relatively greater increment in particulate enzyme as compared with that free in the cytoplasm (non-sedimentable). A small percentage of recovered beta-glucuronidase, acid phosphatase, and alkaline phosphatase is found in material which rises to the surface during centrifugation in sucrose media (fraction I). The specific activity of beta-glucuronidase and acid phosphatase in this fraction is normally quite high with respect to the homogenate, while that of alkaline phosphatase is not. On the other hand, the fraction I material from androgen-stimulated mice exhibits a further increase in specific activity with respect to beta-glucuronidase and not acid phosphatase. It thus appears that there is an independence in the behavior of individual enzymes in response to physiologic stimuli in spite of obvious morphologic proximity.