Abstract
Gonococci were labeled with 125I using the lactoperoxidase system. The amount of label incorporated was similar with all strains including those which appeared capsulated. Electrophoresis on sodium dodecyl sulfate-polyacrylamide gels revealed that the major proteins labeled were those found in outer membrane preparations. Comparison of variants of 1 strain showed that the major outer membrane protein (protein I) was always present and heavily labeled. The 2nd major protein (protein II) was present in variable amounts but labeling was proportional to the amount present. A 3rd protein (III) was only present in outer membranes from a freshly isolated variant but was present in whole cells of each strain. Protein III was not labeled in whole cells but was labeled in outer membrane preparations suggesting that many membranes have their inner surface exposed. The labeling of a strain adapted to growth in guinea-pig chambers failed to reveal any new major surface proteins. The results demonstrate the variation in surface topography possible with variants of 1 strain of gonococcus but show that 1 major protein antigen is always expressed on the surface.