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利用Ferrell和Martin（1991）设计的测定印迹在PVDF膜上的蛋白激酶活性方法研究大豆叶片质膜蛋白激酶自身磷酸化反应活性，结果表明：与Mg－ATP相比，Mn－ATP是更有效的57KD蛋白激酶自身磷酸化反应底物；钙离子可以促进该激酶的自身磷酸化反应活性，而且EGTA可以显著降低它在SDS电泳中的迁移率，说明57KD蛋白激酶为依赖于钙的蛋白激酶；预磷酸化反应实验证明57KD蛋白激酶具有多个自身磷酸化反应位点，其分子的自身磷酸化状态可调性暗示这一激酶可能具有重要的生理功能。
Using the method of Ferrell and Martin (1991) to determine the protein kinase activity of the blot on the PVDF membrane, the autophosphorylation activity of plasma membrane protein kinase in soybean leaves was studied. The results showed that Mn-ATP was more effective than Mg-ATP 57KD protein kinase autophosphorylation reaction substrate; calcium ion can promote the autophosphorylation activity of the kinase, and EGTA can significantly reduce its mobility in the SDS electrophoresis, indicating that 57KD protein kinase is a calcium-dependent protein kinase; pre Phosphorylation experiments show that 57KD protein kinase has multiple autophosphorylation sites, and the self-phosphorylation status of the molecule indicates that this kinase may have important physiological functions.