Kelley J T, Parker C D
J Bacteriol. 1981 Feb;145(2):1018-24. doi: 10.1128/jb.145.2.1018-1024.1981.
Outer membrane proteins of Vibrio cholerae were purified by sucrose density centrifugation and Triton X-100 extraction at 10 mM Mg2+. The proteins were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. V. cholerae outer membrane proteins presented a unique pattern when compared with the patterns of other gram-negative rods. There were 8 to 10 major bands (Mr 94,000 to 27,000), with most of the protein located in band 5 (Mr approximately 45,000), which thus appears to be the major structural protein of the outer membrane. Lipid and carbohydrate were associated with band 6.
霍乱弧菌的外膜蛋白通过在10 mM Mg2+条件下的蔗糖密度离心和Triton X-100提取进行纯化。蛋白质在十二烷基硫酸钠存在下通过聚丙烯酰胺凝胶电泳进行分离。与其他革兰氏阴性杆菌的模式相比，霍乱弧菌外膜蛋白呈现出独特的模式。有8至10条主要条带（分子量94,000至27,000），大部分蛋白质位于条带5（分子量约45,000），因此它似乎是外膜的主要结构蛋白。脂质和碳水化合物与条带6相关。
