An acid-stable hemagglutinin co-purified with potato invertase inhibitor after acid and ammonium sulfate precipitation, hydroxylapatite and DEAE-Sephadex chromatography. The activities were separated by eluting the protein mixture through a glycerol-propylsilane (GPS-) modified silica column in a Tricine buffer. Potato invertase inhibitor was found to have a pI of 5.1. Hemagglutinin activity was associated with a single band that had a pI of 5.6 on IEF-PAGE gels. A second hemagglutinin was isolated in the same preparation with a pI of 8.4. This hemagglutinin showed no affinity for either DEAE-Sephadex or hydroxylapatite. The 2 hemagglutinins were effective against erythrocytes of 4 different species but did not inhibit potato invertase in vitro. Active invertase inhibitor did not agglutinate erythrocytes in vitro. The separate activities of invertase inhibition and erythrocyte hemagglutination are mediated by 3 independent proteins of similar molecular weight (Mr) but different pI values.
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Ovalle et al. (1995) studied this question.
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