N-乙酰咪唑对人红细胞ATP酶活性的影响。关于（钠加钾）依赖性ATP酶的ATP结合位点上酪氨酸残基的证据。

Effects of N-acetylimidazole on human erythrocyte ATPase activity. Evidence for a tyrosyl residue at the ATP binding site of the (Na+ plus K+)-dependent ATPase.

Masiak S J, D'angelo G

Biochim Biophys Acta. 1975 Feb 28;382(1):83-91. doi: 10.1016/0005-2736(75)90375-2.

Abstract

Acetylation of human erythrocytes by N-acetylimidazole alters the structure of stroma prepared from these cells and the degree of alteration appears to be dependent upon the level of the initial treatment. These changes do not occur when stroma are acetylated. 2. Deacetylation by hydroxylamine or mild alkaline treatment causes a complete recovery of the (Na+ plus K+)-dependent and the Ca2+ -stimulated ATPase activities and indicates that the inhibition is due to the acetylation of a tyrosyl residue. There is only partial recovery of the Mg2+ -dependent ATPase after deacetylation. 3. ATP or Mg-ATP completely protect the (Na+ plus K+)-dependent ATPase, but not the Ca2+ -stimulated system. 4. The results indicate that the (Na+ plus K+)-dependent and the Ca2+ -stimulated ATPase activities have separate substrate binding sites and most likely are separate enzyme systems. 5. Acetylation of human erythrocytes has no effect on D-glucose transport.

摘要

N-乙酰咪唑对人红细胞的乙酰化作用改变了由这些细胞制备的基质结构，且改变程度似乎取决于初始处理水平。当基质被乙酰化时，这些变化不会发生。2. 用羟胺或温和碱性处理进行脱乙酰化可使（Na⁺加K⁺）依赖性和Ca²⁺刺激的ATP酶活性完全恢复，这表明抑制作用是由于酪氨酸残基的乙酰化。脱乙酰化后，Mg²⁺依赖性ATP酶仅部分恢复。3. ATP或Mg-ATP可完全保护（Na⁺加K⁺）依赖性ATP酶，但不能保护Ca²⁺刺激的系统。4. 结果表明，（Na⁺加K⁺）依赖性和Ca²⁺刺激的ATP酶活性具有独立的底物结合位点，很可能是独立的酶系统。5. 人红细胞的乙酰化对D-葡萄糖转运没有影响。