Open AccessPurification, characterization, and partial covalent structure of Escherichia coli adhesive antigen K99
Author(s) -
F K de Graaf,
Per Klemm,
Wim Gaastra
Publication year - 1981
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.33.3.877-883.1981
Subject(s) - enterotoxigenic escherichia coli , isoelectric point , escherichia coli , ammonium sulfate precipitation , biology , antigen , size exclusion chromatography , biochemistry , isoelectric focusing , microbiology and biotechnology , enterobacteriaceae , sepharose , enzyme , enterotoxin , gene , genetics
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.
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