Chemical heterogeneity of major outer membrane pore proteins of Escherichia coli.
Peptide mapping and isoelectric focusing were used to compare the major outer membrane pore proteins from various strains of Escherichia coli K-12, including strains carrying mutations in the nmpA, nmpB, and nmpC genes which result in the production of new membrane proteins. Proteins 1a, 1b, and 2 and the NmpA proteins each gave unique peptide and isoelectric focusing profiles, indicating that these are different polypeptides. The NmpA protein and the NmpB protein appeared to be identical by these criteria. The NmpC protein and protein 2 were nearly identical, although one different peptide was observed in comparing the proteolytic peptide maps of these proteins and there were slight differences in their isoelectric focusing profiles. Antiserum against protein 2 showed partial cross-reactivity with the NmpC protein. These results indicate that the various pore proteins of E. coli K-12 fall into four different classes.
D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics; D002473:Cell Wall / Q000032:analysis; D004926:Escherichia coli / Q000032:analysis* / Q000235:genetics; D007526:Isoelectric Point; D008970:Molecular Weight; D009154:Mutation; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation
D001426:Bacterial Proteins; D010455:Peptides