Abstract
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 APase 1 and APase 2 , had pH optima for p -nitrophenyl phosphate hydrolysis around 5.0. APase 1 was inhibited by fluoride, L(+) tartrate, and lead nitrate, but was insensitive to formaldehyde and glutaraldehyde. In contrast, Apase 2 was insensitive to fluoride, L(+) tartrate, and lead nitrate, but was sensitive to formaldehyde and glutaraldehyde. K m values for APase 1 and APase 2 with p -nitrophenyl phosphate as substrate were 0.09mM and 0.125 mM, respectively.
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