Isolation and partial characterization of protein E, a major protein found in certain Escherichia coli K-12 mutant strains: relationship to other outer membrane proteins.
Escherichia coli outer membrane protein E was purified, and its amino acid composition and N-terminal amino acid were determined. The purified protein was shown to be immunologically and electrophoretically identical to proteins Ic (U. Henning, W. Schmidmayr, and I. Hindennach, Mol. Gen. Genet. 154:293-298, 1977) and e (W. van Alphen, N. van Selm, and B. Lugtenberg, Mol. Gen. Genet. 159:75-83, 1978). Proteins E, e, and Ic were also immunologically related to E. coli outer membrane protein Ia. Lugtenberg and co-workers (B. Lugtenberg, R. van Boxtel, C. Verhoef, and W. van Alphen, FEBS Lett. 96:99-105, 1978) have shown that electrophoretically identical peptides were generated by cyanogen bromide treatment of proteins E, e, and Ic.
D000596:Amino Acids / Q000032:analysis; D000942:Antigens, Bacterial / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D004926:Escherichia coli / Q000032:analysis* / Q000276:immunology; D008565:Membrane Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D009154:Mutation
D000596:Amino Acids; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D008565:Membrane Proteins