Shinagawa K, Ueno S, Konuma H, Matsusaka N, Sugii S
Department of Veterinary Medicine, Faculty of Agriculture, Iwate University, Japan.
J Vet Med Sci. 1991 Apr;53(2):281-6. doi: 10.1292/jvms.53.281.
Purification of an extracellular protein exhibiting the vascular permeability activity produced by Bacillus cereus was performed by ammonium sulfate precipitation followed by chromatography on DE-32 cellulose, Sephadex G-100, and Sephadex G-75. The purified protein was found to be electrophoretically and antigenically almost homogeneous although it contained a trace of contaminant. The molecular weight of the protein was calculated to be 45,000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The purified protein showed vascular permeability activity and mouse lethal toxicity, and caused fluid accumulation in ligated mouse intestinal loops, whereas it did not show any hemolytic and lecithinase activities. From these findings, the purified protein is suggested to be an enterotoxin (or a diarrheagenic toxin) responsible for diarrhea caused by B. cereus in a diarrheal-type food poisoning.
对蜡样芽孢杆菌产生的具有血管通透性活性的一种细胞外蛋白进行纯化，方法是先通过硫酸铵沉淀，然后在DE - 32纤维素、葡聚糖G - 100和葡聚糖G - 75上进行层析。尽管纯化后的蛋白含有微量污染物，但经电泳和抗原分析发现其几乎均一。在十二烷基硫酸钠存在的情况下，通过聚丙烯酰胺凝胶电泳计算该蛋白的分子量为45,000。纯化后的蛋白表现出血管通透性活性和小鼠致死毒性，并导致结扎的小鼠肠袢积液，而未表现出任何溶血和卵磷脂酶活性。根据这些发现，推测纯化后的蛋白是一种肠毒素（或致腹泻毒素），在腹泻型食物中毒中导致蜡样芽孢杆菌引起的腹泻。
