Inomata M, Kasai Y, Nakamura M, Kawashima S
Department of Biochemistry, Tokyo Metropolitan Institute of Gerontology, Japan.
J Biol Chem. 1988 Dec 25;263(36):19783-7.
The activation mechanism through limited autolysis of a calcium-activated neutral protease (CANP) with a high sensitivity to calcium ions (microCANP) was analyzed. The rate of autolysis was dependent on microCANP concentration. The reaction was inhibited by high concentrations of digestible substrates but not by a nondigestible substrate. Incubation of microCANP inactivated by N-ethylmaleimide with a small amount of activated microCANP caused the degradation of the former in a manner similar to the autolysis of native microCANP. Immobilized microCANP bound to an anti-microCANP immunoglobulin G column autolyzed on addition of calcium ions. These results show that activation of microCANP through limited autolysis involves both intramolecular and intermolecular reactions.
分析了一种对钙离子高度敏感的钙激活中性蛋白酶（微钙激活中性蛋白酶，microCANP）通过有限自溶的激活机制。自溶速率取决于微钙激活中性蛋白酶的浓度。该反应受到高浓度可消化底物的抑制，但不受不可消化底物的抑制。用少量活化的微钙激活中性蛋白酶孵育被N - 乙基马来酰亚胺灭活的微钙激活中性蛋白酶，会导致前者以类似于天然微钙激活中性蛋白酶自溶的方式降解。固定在抗微钙激活中性蛋白酶免疫球蛋白G柱上的微钙激活中性蛋白酶在添加钙离子后会发生自溶。这些结果表明，通过有限自溶激活微钙激活中性蛋白酶涉及分子内和分子间反应。
