Haddaoui E, Petit-Glatron M F, Chambert R
Institut Jacques Monod, Laboratoire Génétique et Membranes, Paris, France.
J Bacteriol. 1995 Sep;177(17):5148-50. doi: 10.1128/jb.177.17.5148-5150.1995.
Immunoblot analysis of Bacillus subtilis cell extracts with polyclonal antibodies, raised against purified exocellular alpha-amylase, revealed one protein species of 82,000 Da. This protein was found even in cells in which the amyE gene, encoding exocellular alpha-amylase, was disrupted. Isolated from the membrane fraction, the 82,000-M(r) protein displayed an alpha-amylase activity in vitro.
用针对纯化的胞外α-淀粉酶产生的多克隆抗体对枯草芽孢杆菌细胞提取物进行免疫印迹分析,结果显示有一种82,000道尔顿的蛋白质。即使在编码胞外α-淀粉酶的amyE基因被破坏的细胞中也能发现这种蛋白质。从膜组分中分离出的82,000道尔顿(相对分子质量)的蛋白质在体外表现出α-淀粉酶活性。