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ACID HYDROLASES IN THE HUMAN EPIDERMIS
Author(s) -
OHKAWARA AKIRA,
HALRIN KENNETH M.,
TAYLOR JOSEPH R.,
LEVINE VICTOR
Publication year - 1972
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1972.tb01593.x
Subject(s) - glucosidases , acid phosphatase , epidermis (zoology) , biochemistry , enzyme , phosphatase , chemistry , cytoplasm , human skin , microbiology and biotechnology , biology , anatomy , genetics
Summary.— α‐ and β‐D‐glucosidases, β‐D‐glucuronidase, α‐ and β‐D‐mannosidases, α‐and β‐D‐glucosidases, β‐D‐fucosidase, α‐L‐fucosidase and β‐D‐Nacetyglucosaminidase activities were measured in the human epidermis using p‐nitrophenol and 4‐methylumbelliferone compounds as substrates. There was no appreciable difference in activities noted when both substrates were compared. Acid phosphatase was assayed with p‐nitrophenol phosphate and α‐naphthyl acid phosphate as substrates. Acid phosphatase seemed to be present, both free in the cytoplasm and in lysosomes. These 2 activities could not be differentiated by agarose electrophoresis (both fractions showed 2 anodally migrating bands). Some of the biochemical properties of these acid hydrolases from the normal human epidermis are presented.