Acid D-ephedrine-O-phosphatase activity in rate ventral prostate lysosomes.
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.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D004809:Ephedrine; D006651:Histocytochemistry; D008247:Lysosomes / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D011467:Prostate / Q000201:enzymology* / Q000648:ultrastructure; D051381:Rats
D000135:Acid Phosphatase; D004809:Ephedrine