单核细胞增生李斯特菌鞭毛蛋白FlaA的胞壁质水解活性
Murein-hydrolyzing activity of flagellin FlaA of Listeria monocytogenes.
作者信息
Popowska Magdalena, Markiewicz Zdzislaw
机构信息
Department of Bacterial Physiology, Institute of Microbiology, Warsaw University Miecznikowa 1, 02-096 Warsaw, Poland.
出版信息
Pol J Microbiol. 2004;53(4):237-41.
In this preliminary report we show that a 29 kDa surface protein of Listeria monocytogenes EGD removed from cells with 4 M LiCl has peptidoglycan (murein) hydrolyzing activity, as revealed by zymographic analysis using Bacillus subtilis murein and heat-killed Micrococcus luteus cells casted in the gel. Following two-dimensional electrophoresis, the protein was electroblotted to PVDF membrane and its identity (FlaA) was revealed by sequencing. Peptidoglycan hydrolysing activity of FlaA purified by FPLC on Mono-S Sepharose against labelled Escherichia coli murein was demonstrated.
在本初步报告中，我们表明，用4M LiCl从细胞中提取的单核细胞增生李斯特菌EGD的一种29kDa表面蛋白具有肽聚糖（胞壁质）水解活性，这通过使用凝胶中包埋的枯草芽孢杆菌胞壁质和热灭活的藤黄微球菌细胞进行的酶谱分析得以揭示。二维电泳后，该蛋白被电印迹到PVDF膜上，通过测序确定了其身份（FlaA）。还证明了通过FPLC在Mono-S琼脂糖上纯化的FlaA对标记的大肠杆菌胞壁质具有肽聚糖水解活性。
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