Androgens produced by stimulating mouse testis with gonadotropic hormones cause a rise in renal ß-glucuronidase but not an increase in acid or alkaline phosphatase. All subcellular components increase in ß-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 ß-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 ß-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 ß-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.
BETA GLUCURONIDASE-RICH CYTOPLASMIC PARTICLES IN ANDROGEN-STIMULATED MOUSE KIDNEY : A Cytobiochemical Study
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Andrew G. Plaut, William H. Fishman; BETA GLUCURONIDASE-RICH CYTOPLASMIC PARTICLES IN ANDROGEN-STIMULATED MOUSE KIDNEY : A Cytobiochemical Study . J Cell Biol 1 February 1963; 16 (2): 253–258. doi: https://doi.org/10.1083/jcb.16.2.253
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