BIOCHEMICAL OBSERVATIONS ON LEUCINE AMINOPEPTIDASE 2 OF HUMAN SKIN

[摘要] The enzyme in skin which hydro-lyzes leucyl-[beta]-naphthylamide differed from the classical LAP [leucine aminopeptidase] in that it was activated by Co and inhibited by Mn, an activator of LAP-I. Whole skin has substantial amounts of LAP-II (1,000 units/g/hr). While the major portion of the enzyme activity was found in the dermis, the specific activity of the enzyme in the epidermis was 5 to 9 times that of the dermis. Incubation of thin sections of whole skin for 20 min. in buffer resulted in solubilization of about 70 percent of the LAP-II activity.