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Chromatographic Fractionation and Partial Characterization of Acid Phosphatase in Guinea-Pig Epidermis **Department of Department of Dermatology, Kyushu University School of Medicine, Fukuoka, 812, Japan

By Teruo Miyagawa, Hiromu Koda and Harukuni Urabe


Two chromatographically and enzymatically distinct forms of acid phosphatase have been separated by gel filtration from an extract of guinea-pig epidermis. These enzymes, termed APase1 and APase2, had pH optima for p-nitrophenyl phosphate hydrolysis around 5.0. APase1 was inhibited by fluoride, L(+) tartrate, and lead nitrate, but was insensitive to formaldehyde and glutaraldehyde. In contrast, Apase2 was insensitive to fluoride, L(+) tartrate, and lead nitrate, but was sensitive to formaldehyde and glutaraldehyde. Km values for APase1 and APase2 with p-nitrophenyl phosphate as substrate were 0.09mM and 0.125 mM, respectively

Publisher: The Williams & Wilkins Co. Published by Elsevier Inc.
Year: 1974
DOI identifier: 10.1111/1523-1747.ep12680416
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