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  • Title: Isolation, purification, and partial characterization of type V-A hemagglutinin from Escherichia coli GV-12, O1:H-.
    Author: Sheladia VL, Chambers JP, Guevara J, Evans DJ.
    Journal: J Bacteriol; 1982 Nov; 152(2):757-61. PubMed ID: 6752118.
    Abstract:
    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.
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