NDLI: Primary Structure of the CFAl Fimbrial Protein from Human Enterotoxigenic Escherichia coli Strains

Content Provider	Scilit
Author	Klemm, Per
Copyright Year	2005
Description	Journal: Journal of Biological Inorganic Chemistry 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.
Ending Page	348
Starting Page	339
ISSN	2573508X
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1982.tb06597.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	124
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2005-03-03
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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Primary Structure of the CFAl Fimbrial Protein from Human Enterotoxigenic Escherichia coli Strains