Panyim S
Andrologia. 1981 Jul-Aug;13(4):322-9. doi: 10.1111/j.1439-0272.1981.tb00055.x.
The protein kinase in the human seminal plasma, as assayed by its ability to catalyze the transfer of phosphate from [gama-32P]ATP to the protamine, was found to linearly increase with dilution of the seminal plasma. Extrapolation of the enzyme activity to the undiluted seminal plasma indicated that te protein kinase existed in the ejaculate as the inactive enzyme. An inhibitor of the protein kinase was postulated and the results suggested that the inhibitor was a heat-labile macromolecule. However, the linear increase of the protein kinase activity could also be obtained by increasing ATP concentration. In addition, a high Mg+2-dependent ATPase activity was found in the seminal plasma, its activity exhibited inverse relationship with the activity of the protein kinase. The results suggested that the apparent inhibitor of the protein kinase in the human seminal plasma was the destruction of ATP by the ATPase.
通过其催化[γ-32P]ATP的磷酸基团转移至鱼精蛋白的能力来测定，发现人精浆中的蛋白激酶活性随精浆稀释呈线性增加。将酶活性外推至未稀释的精浆表明，该蛋白激酶在射精时以无活性酶的形式存在。推测存在一种蛋白激酶抑制剂，结果表明该抑制剂是一种热不稳定的大分子。然而，增加ATP浓度也可使蛋白激酶活性呈线性增加。此外，在精浆中发现了一种高Mg2+依赖性ATP酶活性，其活性与蛋白激酶活性呈负相关。结果表明，人精浆中蛋白激酶的表观抑制剂是ATP酶对ATP的破坏。
