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
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