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利用电子顺磁共振 (EPR)研究了枯草杆菌中性蛋白酶 (B .S .N .P)与无机Cu(Ⅱ )离子的相互作用 ,结果发现 :枯草杆中性蛋白酶活性中心Zn(Ⅱ )与外加的Cu(Ⅱ )存在着直接相互作用 ,Cu(Ⅱ )可部分置换原酶活性中心Zn(Ⅱ ) ,而进入酶的活性中心Zn(Ⅱ )位 ,形成“Cu N .P”酶衍生物 ,影响了酶的催化活性。此外还发现溶液的pH对相互作用后形成酶衍生物的结构有较大的影响 ,并得到了“Cu N .P”酶衍生物及随pH变化的EPR谱图。
The interaction between Bacillus subtilis neutral protease (B.S.N.P) and inorganic Cu (Ⅱ) ions was studied by electron paramagnetic resonance (EPR). It was found that the activity of Zn (Ⅱ) Cu (Ⅱ) can partially displace Zn (Ⅱ) which is the active site of the original enzyme and enter the Zn (Ⅱ) active site of the enzyme to form “Cu N .P” enzyme derivative , Affecting the catalytic activity of the enzyme. In addition, it was found that the pH of the solution had a great influence on the structure of the enzyme derivative formed after the interaction, and the “Cu N .P” enzyme derivative and the EPR spectrum with the change of pH were obtained.