淋病奈瑟菌外膜蛋白Ⅰ的分离提纯及鉴定

Seperation Purification and Characterization of Outer Membrane Protein Ⅰ of Neisseria Gonorrhoeae

在CaCl2存在下，以CTB提取淋球菌的OMP，再以Z3，14萃取PI，然后经DEAESepharoseCl－6B层析柱提纯，获得纯PI10．97毫克。SDS－PAGE显示纯PI为单一蛋白区带，分子量为35KD，经可见光扫描，其纯度达96.21％。用ELISA间接法检测证明，纯PI保持完好的抗原活性。亚类特异性鉴定证实为WI群PIA。

The outer membrane protein of Neisseria gonorrhoeae was extracted with CTB in presence of CaCl2, then Protein I (P I ) was extracted with Z3, 14 and further purified by DEAE-Sepharose column chromatography. 10. 97mg of pure P I were obtained by this way and detected by SDS-PAGE, and only a single band showed on the electropherogram with a molecular weight of 35KD, Visible light scanning indicated that the purity of P Ireached 96. 21 %. Indirect ELISA proved that the P I remained good antigenicity. The result of subtype specificity identification demonstrated that the P I was subtype A, group W I.