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Purification and Partial Characterization of a Soluble Hemagglutinin from Yersinia pseudotuberculosis
Author(s) -
Takumi Kenji,
Koga Tetsuro,
Oka Tatsuzo,
Takeoka Aya,
Tsubokura Misao,
Sheng Yao Jian
Publication year - 1991
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1991.tb01564.x
Subject(s) - yersinia pseudotuberculosis , isoelectric point , ammonium sulfate precipitation , biology , hemagglutinin (influenza) , peptide sequence , amino acid , size exclusion chromatography , microbiology and biotechnology , escherichia coli , isoelectric focusing , biochemistry , chromatography , chemistry , gene , virulence , enzyme
A soluble hemagglutinin (HA) produced by Yersinia pseudotuberculosis strain Inoue, serotype 5b, was purified by ammonium sulfate precipitation, gel filtration on Sepharose CL‐6B and high performance liquid chromatography on a DEAE‐5PW anion‐exchange column. The purified HA was a 14.5 kDa protein with an isoelectric point of 4.5. Amino acid analysis indicated that the HA consisted of 133 residues, corresponding to the molecular weight of 14,100. The amino acid sequence of N‐terminal 38 amino acid residues showed no homology with that of several fimbrial proteins from Escherichia coli.