sepharose has been researched along with phenylphosphate* in 1 studies
1 other study(ies) available for sepharose and phenylphosphate
| Article | Year |
|---|---|
Purification and some properties of a Mg(2+)-activated acid phosphatase from rat testis.
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. Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Binding Sites; Cations, Divalent; Centrifugation, Density Gradient; Chromatography, Gel; Edetic Acid; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Magnesium; Male; Molecular Weight; Nitrophenols; Organophosphates; Organophosphorus Compounds; Rats; Sepharose; Testis | 1994 |