THE SPECIFICITY OF MACROPHAGE ELASTASE ON THE INSULIN B-CHAIN
THE SPECIFICITY OF MACROPHAGE ELASTASE ON THE INSULIN B-CHAIN
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DOI：
10.1042/bj1950369
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发表时间：
1981-01-01
影响因子：
4.1
通讯作者：
JANOFF, A
中科院分区：
文献类型：
--
作者：
KETTNER, C;SHAW, E;JANOFF, A
从小鼠腹腔渗出性巨噬细胞中获得的巨噬细胞弹性蛋白酶的特异性在氧化胰岛素B链的水解中被确定。这种弹性蛋白酶水解两个键，即Ala-Leu和Tyr-Leu。后者的水解速率是前者的2 ~ 3倍。通过切割胰岛素B链获得的六肽Glu-Ala-Leu-Tyr-Leu-Val不被巨噬细胞弹性蛋白酶水解。当EDTA存在时，未观察到B链的蛋白水解。因此，巨噬细胞弹性蛋白酶在特异性和机制上不同于中性粒细胞弹性蛋白酶。
The specificity of macrophage elastase obtained from mouse peritoneal exudative macrophages was determined in the hydrolysis of the oxidized insulin B-chain. This elastase hydrolysed two bonds, namely Ala-Leu and Tyr-Leu. The rate of hydrolysis of the latter was two to three times greater than that of the former. The hexapeptide Glu-Ala-Leu-Tyr-Leu-Val, obtained by cleavage of the insulin B-chain, was not hydrolysed by macrophage elastase. When EDTA was present, proteolysis of the B-chain was not observed. The macrophage elastase is therefore different from the neutrophil elastase in specificity and mechanism.