Chanter N, Rutter J M, Mackenzie A
J Gen Microbiol. 1986 Apr;132(4):1089-97. doi: 10.1099/00221287-132-4-1089.
A protein toxin apparently composed of one polypeptide with an estimated Mr of 155,000 was purified from sonicated cells of a type D strain of Pasteurella multocida (LFB3) by preparative polyacrylamide gel electrophoresis (PAGE) and DEAE-Sephadex A50 chromatography. Its specific activity was 150-fold greater than that of the crude extract. The partially purified protein was cytotoxic for embryonic bovine lung cells, lethal for mice and caused turbinate atrophy in gnotobiotic pigs; a single intraperitoneal injection of approximately 360 ng kg-1 caused 50% turbinate atrophy. Reversal of the two-step purification procedure using DEAE-Sephacel chromatography followed by preparative PAGE increased the yield of toxin 30-fold; the specific activity of the partially purified toxin was 1970-fold greater than that of the crude extract.
一种明显由一条多肽组成、估计相对分子质量为155,000的蛋白质毒素，通过制备性聚丙烯酰胺凝胶电泳（PAGE）和DEAE-葡聚糖凝胶A50层析，从多杀巴斯德菌D型菌株（LFB3）的超声破碎细胞中纯化得到。其比活性比粗提物高150倍。部分纯化的蛋白质对胚胎牛肺细胞具有细胞毒性，对小鼠具有致死性，并导致无菌猪的鼻甲萎缩；单次腹腔注射约360 ng kg-1可导致50%的鼻甲萎缩。使用DEAE-琼脂糖凝胶层析随后进行制备性PAGE的两步纯化程序的反转，使毒素产量提高了30倍；部分纯化毒素的比活性比粗提物高1970倍。
