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PMID: 7026448 Published · ppublish English Journal Article

Purification, characterization, and partial covalent structure of Escherichia coli adhesive antigen K99.

Infection and immunity ·Vol. 33 ·No. 3 ·1981-09-00 ·Pages 877-83

de Graaf FK, Klemm P, Gaastra W

Abstract

The adhesive antigen K99 of enterotoxigenic Escherichia coli strains of calf origin was isolated and purified. The K99 fimbriae were removed from the cells by heat treatment, concentrated by precipitation with ammonium sulfate, and purified by gel filtration on Sepharose CL-4B and treatment with deoxycholate. The purified K99 antigen was composed of protein subunits with a molecular weight of 18,500 and had an isoelectric point of 9.5. The N-terminal amino acid sequence, as well as the composition of the C-terminal part of the K99 protein subunits, was determined.

MeSH Terms
Adhesiveness Amino Acid Sequence Amino Acids/analysis Antigens, Bacterial/analysis,isolation & purification Escherichia coli/immunology Isoelectric Point Molecular Weight
Chemicals
Amino Acids Antigens, Bacterial
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
de Graaf F K
Klemm P
Gaastra W
References (20)
20 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.33.3.877-883.1981
Published
1981-09-00
Pages
877-83
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC350793
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.33.3.877-883.1981 PMC Full Text View journal details
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