Proteolytic activity of largomycin.
Proteolytic activity of largomycin.
复制标题
拉戈霉素的蛋白水解活性。
DOI：
10.1016/0304-4165(85)90067-4
复制
发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Montgomery,R
中科院分区：
文献类型：
--
作者：
Zaheer,A;Zaheer,S;Montgomery,R
Largomycin, an antibiotic and antitumor protein, purified from the culture broth ofStreptomyces pluricolorescens, displayed specific proteolytic activity. Pure largomycin did not degrade a number of substrates commonly used for detection of aminopeptidase, endopeptidase and carboxypeptidase activity. Pure largomycin degraded angiotensin II, bradykinin, a few dipeptides and a number of proteins of KB cell plasma membranes. The biological activity and the proteolytic activity of largomycin showed similar temperature-dependent patterns, suggesting that one protein in responsible for both activities. The apoprotein of largomycin, which did not show antibiotic activity, contained the proteolytic activity.
