Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 66:375-378 (1980)
© 1980 American Society of Plant Biologists

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Articles

Legume

{alpha}-GALACTOSIDASE FORMS DEVOID OF HEMAGGLUTININ ACTIVITY

Charles N. Hankins, Juanita I. Kindinger and Leland M. Shannon

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

Twenty different legume species (20 genera) were examined for {alpha}-galactosidase and hemagglutinin activities. Although all of the species contained enzyme activity, only 13 of 20 contained hemagglutinin activities and none displayed a hemagglutinin activity comparable to the previously described {alpha}-galactosidase-hemagglutinins.

The {alpha}-galactosidase activities in the 20 species possessed remarkably similar kinetic behavior and carbohydrate specificities. All were inhibited by galactose, xylose, and inositol (very similar Ki values from plant to plant) and had very similar Km values for the substrate, p-nitrophenyl {alpha}-galactoside.

Gel filtration analysis of extracts from nine species suggests that legume {alpha}-galactosidase activities may frequently reside in two molecular weight forms. However, all these species contained a large molecular weight enzyme activity with a size comparable to the {alpha}-galactosidase-hemagglutinins.

Immunochemical studies reveal that the {alpha}-galactosidases in these plants are immunologically related to an {alpha}-galactosidase-hemagglutinin and, therefore, are related to one another.

These studies suggest that each of the legume species studied (and perhaps all members of this plant family) contain a homologue from a specific class of {alpha}-galactosidase. Although the previously described {alpha}-galactosidase-hemagglutinins appear to be members from this enzyme class, these proteins most frequently occur as forms devoid of hemagglutinin activity.








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