Acid-stable hemagglutinin proteins co-purifying with potato invertase inhibitor

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 Tr...

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Bibliographic Details
Published in:Plant science (Limerick) 1995-06, Vol.108 (2), p.133-141
Main Authors: Ovalle, Rafael, Keyes, Alan C., Ewing, Elmer E., Quimby, Fred W.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Enzymes
Fundamental and applied biological sciences. Psychology
Hemagglutinin
HPLC
Inhibitor
Invertase
Metabolism
Plant physiology and development
Potato
Purification
Size exclusion
Solanaceae
Solanum tuberosum
Tricine
Zwitterion
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Summary: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 p I of 5.1. Hemagglutinin activity was associated with a single band that had a p I of 5.6 on IEF-PAGE gels. A second hemagglutinin was isolated in the same preparation with a p I 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 ( M r) but different p I values.
ISSN:0168-9452
1873-2259
DOI:10.1016/0168-9452(95)04145-K