Hun S C, Bucher D, Kharitonenkov I G
Vopr Virusol. 1991 Sep-Oct;36(5):381-4.
The degree of solubility of influenza virus protein M1 preparations isolated from virions by acid chloroform-methanol extraction was studied under the effect of a wide spectrum of detergents of different origin. The same detergents were used for solution of a lipid comprising a part of artificially formed liposomes. Only some of the detergents used (sodium dodecyl sulfate, SDS, triton X-100, and disintegron-B) were shown to be optimal for solution of both influenza virus protein M1 and lipid. The degree of effect on the immunochemical properties of protein ML isolated from influenza virus virion of the above-mentioned detergents optimal for solution was also studied. For this purpose, a panel of 18 monoclonal antibodies with different determinant specificity to protein M1 was used. Two of the three detergents (SDS and disintegron-B) were shown not to change the antigenic profile of protein M1. The immunochemical properties of protein M1 of influenza virus isolated from virions by two methods: chloroform-methanol extraction and preparative polyacryl amide gel electrophoresis, were studied. These two methods of protein M1 isolation were shown not to alter its immunochemical properties.
研究了通过酸性氯仿 - 甲醇萃取从病毒粒子中分离出的流感病毒蛋白M1制剂在多种不同来源去污剂作用下的溶解度。相同的去污剂用于溶解构成人工形成脂质体一部分的脂质。结果表明,仅所用的某些去污剂(十二烷基硫酸钠、SDS、曲拉通X - 100和去整合素 - B)对流感病毒蛋白M1和脂质的溶解都是最佳的。还研究了上述对溶解最佳的去污剂对从流感病毒粒子中分离出的蛋白M1免疫化学性质的影响程度。为此,使用了一组对蛋白M1具有不同决定簇特异性的18种单克隆抗体。三种去污剂中的两种(SDS和去整合素 - B)显示不会改变蛋白M1的抗原谱。研究了通过两种方法从病毒粒子中分离流感病毒蛋白M1的免疫化学性质:氯仿 - 甲醇萃取和制备性聚丙烯酰胺凝胶电泳。结果表明,这两种蛋白M1分离方法不会改变其免疫化学性质。