Purification and characterization of guinea-pig epidermal acid phosphatase
- 1 March 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in British Journal of Dermatology
- Vol. 96 (3), 263-270
- https://doi.org/10.1111/j.1365-2133.1977.tb06135.x
Abstract
Guinea-pig epidermal acid phosphatase was purified approximately 120-fold by a procedure including acid treatment, CM-cellulose and DEAE-cellulose chromatography and gel filtration on Sephadex G-100. The enzyme had a pH optimum at 5.0 and the optimal temperature for activity was approximately 50.degree. C. The enzyme was not activated by divalent cations or 2-mercaptoethanol, but it was inhibited by p-chloromercuribenzoate and by F-. The Km value for p-nitrophenyl phosphate was 1.31 .times. 10-4 M; the MW was about 73,000 as determined by Sephadex G-100 gel filtration and the isoelectric point was 6.1. The enzyme hydrolyzed deoxyribonucleoside monophosphates to deoxyribonucleosides.This publication has 9 references indexed in Scilit:
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