Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
British journal of dermatology
96 (1977), S. 0
ISSN:
1365-2133
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Guinea-pig epidermal acid phosphatase has been 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 C. The enzyme was not activated by divalent cations or 2-mercaptoethanol, but it was inhibited by p-chloromercuribenzoate and by fluoride. The km value for p-nitrophenyl phosphate was 1.31 × 10−4 M, the molecular weight 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2133.1977.tb06135.x
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