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PMID: 6124420 Published · ppublish English Journal Article

Primary structure of the CFA1 fimbrial protein from human enterotoxigenic Escherichia coli strains.

European journal of biochemistry ·Vol. 124 ·No. 2 ·1982-05-17 ·Pages 339-48

Klemm P

Abstract

The complete amino acid sequence of the structural protein that constitutes the subunit of the CFA1 fimbria has been elucidated. The protein was fragmented by cyanogen bromide cleavage, and by enzymatic cleavage with trypsin. Secondary cleavage of the resulting peptides was performed with chymotrypsin, Staphylococcus aureus protease, and thermolysin. Sequential Edman degradation was performed manually. The CFA1 protein comprises 147 amino acid residues, with a molecular weight of 15058.

MeSH Terms
Amino Acid Sequence Antigens, Bacterial/isolation & purification Cyanogen Bromide Diarrhea/microbiology Escherichia coli/analysis,isolation & purification Fimbriae Proteins Fimbriae, Bacterial/analysis Humans Peptide Fragments/analysis
Chemicals
Antigens, Bacterial Peptide Fragments colonization factor antigens Fimbriae Proteins Cyanogen Bromide
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Klemm P
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1982-05-17
Pages
339-48
Language
English
Region
England
NLM ID
0107600
Subset
IM
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