PARTIAL PURIFICATION AND CHARACTERIZATION OF THE MAJOR OUTER MEMBRANE PROTEIN OF NEISSERIA GONORRHOEAE
淋球菌主要外膜蛋白的部分纯化与鉴定

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.