Open AccessThe Major Proteins of the Escherichia coli Outer Cell‐Envelope Membrane
Author(s) -
GARTEN Wolfgang,
HINDENNACH Ingrid,
HENNING Ulf
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb21004.x
Subject(s) - escherichia coli , cell envelope , envelope (radar) , bacterial outer membrane , membrane , microbiology and biotechnology , membrane protein , chemistry , cell , biophysics , biology , biochemistry , computer science , gene , telecommunications , radar
The cyanogen bromide fragments of protein I, a major protein of the Escherichia coli outer cell envelope membrane, have been isolated and characterized. There appear to be two methionineserine or methionine‐threonine sequences causing incomplete cleavage but complete conversion of methionine to homoserine. Largely due to the existence of these overlapping fragments the order of 5 of the 6 fragments present could be deduced. None of the fragments exhibits any remarkable low degree of polarity, and the tryptic fingerprint of the largest fragment (comprising about 60% of protein I) also does not show any conspicuous large fraction of lipophilic peptides. It is concluded that the domain of protein I that may be buried in the lipid phase of the outer membrane in all likelihood is not very large, and there is, in fact, no definite proof yet that protein I is a membrane protein sensu stricto.