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ENZYMOLOGICAL STUDIES OF EPIDERMAL ACID PHOSPHATASE
Author(s) -
Miyagawa Teruo,
Nakayama Juichiro,
Toshitani Shoji,
Ogura Ryohei
Publication year - 1978
Publication title -
the journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.9
H-Index - 65
eISSN - 1346-8138
pISSN - 0385-2407
DOI - 10.1111/j.1346-8138.1978.tb01855.x
Subject(s) - ethylenediaminetetraacetic acid , acid phosphatase , tartrate , sephadex , chemistry , enzyme , biochemistry , epidermis (zoology) , phosphatase , chromatography , size exclusion chromatography , divalent , phosphate , biology , chelation , organic chemistry , anatomy
Acid phosphatase of newborn rat epidermis was purified about 270‐fold by a procedure including acid treatment, CM‐cellulose, DEAE‐cellulose chromatography, and gel filtration on Sephadex G‐100. The purified enzyme had a pH optimum of 5.0 and an optimal temperature of 40°C. The enzyme was not activated by divalent cations, ethylenediaminetetraacetic acid or 2‐mercaptoethanol, and it was inhibited by p‐chloromercuribenzoate. The inhibition pattern by fluoride and by L(+) tartrate was competitive. The Km value for p‐nitrophenyl phosphate was 3.84×10 −5 M, and the molecular weight was about 73, 000. The enzyme appeared to be a nonspecific acid phosphatase. Intracellular localization of acid phosphatase in the epidermis was discussed.