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• W1970147658 abstract "1. The acid phosphatase (AcPase, EC 3.1.3.2) IV from rat testicular tissue was purified to apparent homogeneity. 2. The enzyme displays a native molecular weight of 70 kDa determined on gel permeation chromatography on a Sephadex G-100 column and 68 kDa using linear 5-20% sucrose density gradient centrifugation. The subunit molecular weight on SDS-PAGE analysis is 67 kDa, suggesting that the enzyme is a monomeric protein. 3. The enzyme does not bind to Concanavaline A-Sepharose 4B column, indicating that it is not a glycoprotein. 4. The rat testis AcPase IV is a metal activated enzyme in which Mg2+ is the metal activating agent with a Ka = 0.88 x 10(-3) M. The Michaelis constant for p-nitrophenylphosphate, in the presence of saturating concentrations of Mg2+ ions, is 0.23 x 10(-3) M. 5. The enzyme preferentially hydrolyzes p-nitrophenylphosphate, phenylphosphate and ATP." @default.
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• W1970147658 date "1994-07-01" @default.
• W1970147658 modified "2023-09-26" @default.
• W1970147658 title "Purification and some properties of a Mg2+-activated acid phosphatase from rat testis" @default.
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• W1970147658 doi "https://doi.org/10.1016/0020-711x(94)90081-7" @default.
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