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Structural and functional properties of colicin M.

机译:大肠菌素M的结构和功能特性

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Colicin M of Escherichia coli Cl139 was isolated in pure form. It consisted of a single polypeptide with a molecular weight of 27,000 +/- 2,000. Colicin M lysed sensitive cells of E. coli but had to act continuously up to the point when lysis commenced (after 20 min). Colicin M was largely resistant to hydrolysis by trypsin except when adsorbed to cells. Within 4 to 5 min after addition of colicin M, cells could be rescued by trypsin or sodium dodecyl sulfate. Later, colicin M was apparently inaccessible to these inactivating agents. Killing of cells by colicin M required Ca2+ ions. Cells could be rescued with ethylene glycol-bis(beta-aminoethyl ether)-N,N'-tetraacetate (EGTA) immediately before the onset of lysis. Under these conditions, colicin M remained bound to the cells, and it became again sensitive to trypsin. We conclude that under the influence of EGTA colicin M is removed from its site of action and becomes again accessible to trypsin at the cell surface.
机译:以纯净形式分离出大肠杆菌Cl139的ColicinM。它由分子量为27,000 +/- 2,000的单个多肽组成。 Colicin M裂解了大肠杆菌的敏感细胞,但必须持续作用直至裂解开始(20分钟后)。 Colicin M除吸附到细胞外,对胰蛋白酶的水解具有很大的抵抗力。加入大肠菌素M后4至5分钟内,可通过胰蛋白酶或十二烷基硫酸钠拯救细胞。后来,大肠菌素M显然无法进入这些灭活剂。大肠菌素M杀死细胞需要Ca2 +离子。裂解开始前,可用乙二醇-双(β-氨基乙基醚)-N,N'-四乙酸酯(EGTA)拯救细胞。在这些条件下,大肠菌素M仍与细胞结合,并再次对胰蛋白酶敏感。我们得出的结论是,在EGTA的影响下,大肠菌素M从其作用位点移出,并再次在细胞表面变为胰蛋白酶可及的。

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