IDENTIFICATION BY MEANS OF L-PHENYLALANINE INHIBITION OF INTESTINAL ALKALINE PHOSPHATASE COMPONENTS SEPARATED BY STARCH GEL ELECTROPHORESIS OF SERUM.
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Biomedical subjects
Publications and source records attributed to W H FISHMAN.
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Glycogen synthetase activity in the livers of starved mice is stimulated by the glucocorticoid, cortisol.
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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.
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