M A Geffert

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Hydrolysis of D-ephedrine-O-phosphate (DEP) by rat ventral prostrate was investigated by electron microscopic hystochemistry. In contrast to previous reports that DEP is exclusitely hydrolyzed by a secreted nonlysosomal acid phosphatase, enzyme reaction product was present in supranuclear and basal lysosomes.
The histochemical demonstration of acid phosphatase activities against phosphoethanolamine (PEA), phosphorylcholine (PC), and D-ephedrine phosphate (DEP) are reported for a variety of rat tissues and are compared to acid beta-glycerophosphatase (beta GPase) activity. Intense acid beta GPase activity was demonstrated in all tissues examined. However, liver,(More)
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