淋球菌主要外膜蛋白的部分纯化与鉴定  

PARTIAL PURIFICATION AND CHARACTERIZATION OF THE MAJOR OUTER MEMBRANE PROTEIN OF NEISSERIA GONORRHOEAE

作　　者：刘先洲[1] 蒋正明[1] 白瑞珍[1] 汤纪路[1] 张秋萍[1] 

机构地区：[1]湖北医科大学微生物学教研室,武汉430071

出　　处：《微生物学通报》2000年第1期28-30,共3页Microbiology China

摘　　要：应用国产十六烷基三甲基溴化铵提取淋球菌外膜蛋白Ｉ（ＰＩ），继用Ｓｅｐｈａｒｏｓｅ ６Ｂ纯化，并通过ＳＤＳ－ＰＡＧＥ鉴定所提ＰＩ的纯度，以及用琼脂双扩散法测定其抗原性。该法提取淋球菌ＰＩ的纯度高，收获量大，对抗原结构无破坏，适宜在淋球菌的生物学研究中应用。Major outer membrane protein (PI) of Neisseria gonorrhoeae was isolated in large quantities by precipitation with hexadecyltrimethylammoniurm bromide, and substantially purified by chromatography over Sepharose 6B. PI purity was assessed by SDS-PAGE and its capacity reacting to antibody was detected by immunodiffusion. The purifying results suggest that the procedures for isolating the PI of Neisseria gonorrhocae is efficient in purity and yield, and the purified PI obtained by this method maintain their original structure.

关 键 词：淋球菌 外膜蛋白 纯化 鉴定 

分 类 号：Q939.91[生物学—微生物学]