title: Studies on gonococcus infection. XVIII. 125I-labeled peptide mapping of the major protein of the gonococcal cell wall outer membrane.
abstract: The major outer membrane proteins from 10 gonococcal strains were examined after 125I-labeling of the proteins as single bands resolved by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. These 125I-proteins were then treated with either trypsin or alpha-chymotrypsin, and the resultant 125I-peptides were visualized by autoradiography after two-dimensional electrophoretic and chromatographic separation on thin-layer cellulose sheets. Several 125I-peptides were present in all the major outer membrane proteins examined. The presence and absence of additional 125I-peptides segregated the major proteins into two pattern groups. One group consisted of major outer membranes with molecular weights of 34,000 or 33,000; major proteins with molecular weights of 32,000 constituted the other group. Two beta-lactamase-producing gonococcal isolates were examined. Their major outer membrane proteins were identical in apparent molecular weights and alpha-chymotryptic 125I-peptide fingerprints; these proteins contained 125I-peptides not found in other gonococcal major proteins. No 125I-peptide differences were found among the major outer membrane proteins of strain F62 gonococci that exhibited differences in piliation and/or colony opacity characteristics.
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis*; D002918:Chymotrypsin; D006069:Gonorrhea / Q000382:microbiology; D008565:Membrane Proteins / Q000032:analysis*; D009344:Neisseria gonorrhoeae / Q000032:analysis* / Q000201:enzymology / Q000648:ultrastructure; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D013499:Surface Properties; D001618:beta-Lactamases / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D002918:Chymotrypsin; D001618:beta-Lactamases