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.
D000135:Acid Phosphatase; D000469:Alkaline Phosphatase; D000715:Anatomy; D000728:Androgens; D000818:Animals; D003593:Cytoplasm; D005966:Glucuronidase; D007668:Kidney; D008297:Male; D051379:Mice
D000728:Androgens; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D005966:Glucuronidase
ANATOMY; GLUCURONIDASE; KIDNEY