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肺炎克雷伯菌一种约70千道尔顿蛋白质的ADP核糖基化作用。

ADP-ribosylation of an approximately 70-kilodalton protein of Klebsiella pneumoniae.

作者信息

Geipel U, Just I, Aktories K

机构信息

Abteilung Bakteriologie und Hygiene, Institut für Medizinische Mikrobiologie und Hygiene, Homburg/Saar, Germany

出版信息

Infect Immun. 1996 May;64(5):1720-3. doi: 10.1128/iai.64.5.1720-1723.1996.

Abstract

An approximately 70-kDa protein in the culture supernatant of a human pathogenic strain of Klebsiella pneumoniae was labeled in the presence of [32P-adenylate]NAD. Labeling was significantly increased by the addition of dithiothreitol ( > 1 mM) but prevented by treatment of the culture supernatant for 3 min at 56 degrees C. The addition of unlabeled NAD, but not of ADP-ribose, blocked labeling of the approximately 70-kDa protein. The radioactive label was released by formic acid but not by HgCl2 (1 mM) or neutral hydroxylamine (0.5 M). The addition of homogenates of human platelets, human neutrophils, rat brain, rat lung, or rat spleen tissues to the culture supernatant did not induce labeling of eukaryotic proteins. The data indicate that the K. pneumoniae strain produces ADP-ribosyltransferase which modifies an endogenous protein.

摘要

在[32P-腺苷酸]NAD存在的情况下,对一株人致病性肺炎克雷伯菌培养上清液中的一种约70 kDa的蛋白质进行了标记。添加二硫苏糖醇(>1 mM)可显著增加标记,但在56℃处理培养上清液3分钟可阻止标记。添加未标记的NAD而非ADP-核糖可阻断约70 kDa蛋白质的标记。放射性标记可被甲酸释放,但不能被HgCl2(1 mM)或中性羟胺(0.5 M)释放。将人血小板、人中性粒细胞、大鼠脑、大鼠肺或大鼠脾组织的匀浆添加到培养上清液中不会诱导真核蛋白质的标记。数据表明,肺炎克雷伯菌菌株产生ADP-核糖基转移酶,该酶可修饰一种内源性蛋白质。

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