Open AccessIsolation, purification, and partial characterization of type V-A hemagglutinin from Escherichia coli GV-12, O1:H-
Author(s) -
V L Sheladia,
James P. Chambers,
Johnny Guevara,
Doyle J. Evans
Publication year - 1982
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.152.2.757-761.1982
Subject(s) - hemagglutinin (influenza) , biology , escherichia coli , molecular mass , polyacrylamide gel electrophoresis , sodium dodecyl sulfate , gel electrophoresis , immunoelectrophoresis , biochemistry , mannose , sephadex , microbiology and biotechnology , chromatography , chemistry , enzyme , antibody , gene , immunology
A hemagglutinin which specifically agglutinates human type A erythrocytes (mannose resistant) was isolated from the growth medium of cultures of Escherichia coli GV-12, serotype O1:H-, and purified by chromatography on Bio-Gel A-1.5 and DEAE-Sephadex A-25. The purity of the hemagglutinin was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoelectrophoresis. N-terminus analysis indicated that only asparagine resides on the amino terminus. The native hemagglutinin is an aggregate exhibiting a sedimentation coefficient of 9.25, which corresponds to a molecular weight of approximately 200,000. The monomeric molecular weight was found to be approximately 16,300. Amino acid analysis indicated that the hemagglutinin consists of 131 residues, corresponding to a molecular weight of 13,400.