Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 69:628-631 (1982)
© 1982 American Society of Plant Biologists

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Articles

An {alpha}-Galactosidase with Hemagglutinin Properties from Soybean Seeds 1

Elena del Campillo2 and Leland M. Shannon

Department of Biochemistry, University of California, Riverside, California 92521

Soybean (Glycine max L.) seeds contain a galactose-binding protein which displays two activities: (a) an {alpha}-galactosidase activity and (b) a hemagglutinin activity. The {alpha}-galactosidase-hemagglutinin was purified to homogeneity by conventional protein purification procedures and also by affinity chromatography. This protein can be easily separated from soybean agglutinin, the N-acetyl-D-galactosamine-specific lectin in soybean. Further, these two agglutinins show no immunological relatedness. The {alpha}-galactosidase-hemagglutinin can be reversibly converted by pH changes from a tetrameric form which displays both enzymic and hemagglutinin activities to a monomeric form which displays enzymic activity only. Although both the monomeric and tetrameric forms are enzymically active, they display different pH optima and carbohydrate specificities.

2 Recipient of a Fulbright Fellowship and The Delta Kappa Gamma Society International Award.

1 The work described here is from a dissertation submitted in 1980 by Elena del Campillo to the Graduate Division of the University of California, Riverside, in partial fulfillment of the requirements for the Ph.D. Degree. Portions of the work were sponsored by Grant PCM 7901450-01 from the National Science Foundation.




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 J Exp BotHome page
J. A. Feurtado, M. Banik, and J. D. Bewley
The cloning and characterization of {{alpha}}-galactosidase present during and following germination of tomato (Lycopersicon esculentum Mill.) seed
J. Exp. Bot., June 1, 2001; 52(359): 1239 - 1249.
[Abstract] [Full Text] [PDF]


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Copyright © 1982 by the American Society of Plant Biologists