Purification of Neisseria gonorrhoeae surface L-antigen.

A purified preparation of the L-antigen of Neisseria gonorrhoeae with a 40-fold increase of antigenic activity over the crude extract was prepared. The antigen was extracted from the cell envelope by mild treatment with sodium dodecyl sulfate and purified by Sepharose 4B, diethylaminoethyl-cellulose, and diethyl-(2-hydroxypropyl)aminoethyl (QAE)-Sephadex column chromatography. The purified antigen was heat labile and trypsin sensitive. The smallest antigenically active subunit appeared to have a molecular weight of 38,500, as shown by polyacrylamide gel electrophoresis of the product incubated with sodium dodecyl sulfate.