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PMID: 7049161 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.

The Biochemical journal ·Vol. 203 ·No. 1 ·1982-04-01 ·Pages 33-43

Chen R, Krämer C, Schmidmayr W, Chen-Schmeisser U, Henning U

Abstract

In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.

MeSH Terms
Amides/analysis Amino Acid Sequence Bacterial Outer Membrane Proteins Chromatography, Gel Cyanogen Bromide Escherichia coli/analysis Membrane Proteins Peptide Fragments/isolation & purification Trypsin Tryptophan/analysis
Chemicals
Amides Bacterial Outer Membrane Proteins Membrane Proteins Peptide Fragments Tryptophan Trypsin Cyanogen Bromide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Chen R
Krämer C
Schmidmayr W
Chen-Schmeisser U
Henning U
References (33)
33 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2030033
Published
1982-04-01
Pages
33-43
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1158189
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2030033 PMC Full Text View journal details
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