一种来自大鼠肠道平滑肌的中性蛋白酶的低分子量抑制剂。
A low-molecular-weight inhibitor of the neutral proteinase from rat intestinal smooth muscle.
作者信息
Carney I T, Curtis C G, Kay J K, Birket N
出版信息
Biochem J. 1980 Feb 1;185(2):423-33. doi: 10.1042/bj1850423.
Abstract
- Rat intestinal smooth muscle was shown to contain endogenous inhibitory activity towards the neutral trypsin-like muscle proteinase described previously [Beynon & Kay (1978) Biochem. J. 173, 291--298]. 2. Comtamination of the muscle tissue by mucosal, blood and pancreatic inhibitors was shown to be unlikely. 3. The inhibitory activity was resolved into high- and low-molecular-weight components. 4. The low-molecular-weight component was purified to homogeneity. It has a molecular weight of approx. 9000 and was stable over the pH range 3--11. 5. It inhibited the muscle proteinase competitively (Ki congruent to t microM), but had no effect on any of the other proteinases tested. 6. Leupeptin also inhibited the muscle proteinase competitively (Ki congruent to 0.3 microM), whereas the low-molecular weight proteins gastrin, glucagon and insulin B-chain had very little effect. 7. A role for a weakly binding inhibitor in modulating the influence of the neutral proteinase on intracellular protein degradation is considered.
摘要
- 已证明大鼠肠道平滑肌含有对先前所述的中性类胰蛋白酶样肌肉蛋白酶的内源性抑制活性[贝农和凯（1978年），《生物化学杂志》173卷，291 - 298页]。2. 已表明肌肉组织不太可能受到黏膜、血液和胰腺抑制剂的污染。3. 抑制活性被分离为高分子量和低分子量组分。4. 低分子量组分被纯化至同质。其分子量约为9000，在pH值3至11范围内稳定。5. 它竞争性抑制肌肉蛋白酶（Ki约为1 microM），但对所测试的任何其他蛋白酶均无作用。6. 亮肽素也竞争性抑制肌肉蛋白酶（Ki约为0.3 microM），而低分子量蛋白质胃泌素、胰高血糖素和胰岛素B链的作用很小。7. 考虑了一种弱结合抑制剂在调节中性蛋白酶对细胞内蛋白质降解影响方面的作用。
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