枯草芽孢杆菌中一种钙结合蛋白的鉴定与纯化。

Identification and purification of a calcium-binding protein from Bacillus subtilis.

作者信息

Tozzi M G, D'Arcangelo U, Del Corso A, Ordal G W

机构信息

Dipartimento di Fisologia e Biochimica, Laboratori di Biochimica, Pisa, Italy.

出版信息

Biochim Biophys Acta. 1991 Oct 25;1080(2):160-4. doi: 10.1016/0167-4838(91)90144-o.

DOI:10.1016/0167-4838(91)90144-o

PMID:1932092

Abstract

A Ca(2+)-binding protein was identified in Bacillus subtilis in the log phase of growth. The molecular mass of this protein is about 38 kDa as estimated by polyacrylamide gel electrophoresis in the presence of SDS and by gel filtration. The protein was found to be resistant 10 min at 65 degrees C and was purified about 400 times, starting from heated crude extract, by conventional procedures. This novel protein is able to bind Ca2+ in the presence of an excess of MgCl2 and KCl both in solution and after SDS gel electrophoresis and electrotransfer. Since an impairment of the Ca2+ intake, in Bacillus subtilis, results in an impairment of chemotactic behavior (Matsushita, T. et al (1988) FEBS lett. 236, 437-440), 38 kDa protein may be involved in the regulation of chemotaxis.

摘要

在枯草芽孢杆菌生长的对数期鉴定出一种钙结合蛋白。通过在SDS存在下的聚丙烯酰胺凝胶电泳和凝胶过滤估计，该蛋白的分子量约为38 kDa。发现该蛋白在65℃下10分钟具有抗性，并且通过常规程序从加热的粗提取物开始纯化约400倍。这种新型蛋白在溶液中以及SDS凝胶电泳和电转移后，在过量的MgCl2和KCl存在下能够结合Ca2+。由于枯草芽孢杆菌中Ca2+摄取的损害会导致趋化行为的损害（松下，T.等人（1988年）FEBS lett. 236, 437 - 440），38 kDa蛋白可能参与趋化性的调节。