Lectin in five soybean cultivars previously considered to be lectin-negative |
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Authors: | H C Tsien Michele A Jack E L Schmidt Finn Wold |
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Institution: | (1) Department of Microbiology, University of Minnesota, 55455 Minneapolis, MN, USA;(2) Department of Biochemistry, University of Minnesota, 55108 St. Paul, MN, USA;(3) Present address: Department of Biochemistry and Molecular Biology, University of Texas, Health Science Center, 77025 Houston, TX, USA |
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Abstract: | Hemagglutinating proteins were isolated by affinity chromatography from seeds of each of five cultivars of soybeans (Clycine max (L.) Merr.) previously reported to lack detectable lectin (S.P. Pull et al., 1978; Science 200, 1277). Quantities were between 1,000 and 10,000 times less than that found in the seeds of the reference cultivar, Chippewa. The sensitivity of the hemagglutinating assay was 0.05 g ml-1. Hemagglutinating activity was demonstrated in affinity-purified fractions from bulk seeds and seeds from individual plants in two cultivars, 30–70% ammonium-sulfate-precipitable fractions of seeds from individual plants of all five cultivars, and in whole crude extracts of individual seeds from each cultivar. In all instances, hemagglutinating activity was inhibited by galactose, anti-soybean agglutinin (SBA), and lectin-binding polysaccharide produced by Rhizobium japonicum. Affinity-purified lectin from seeds of a single Columbia plant was labeled with fluorescein isothiocyanate (FITC) and observed by fluorescence microscopy to bind to R. japonicum cells with specificity, intensity and localization indistinguishable from FITC-SBA. Lectins from distinguishable from FITC-SBA. Lectins from three cultivars in sufficiently high concentration for study had molecular properties very similar to Chippewa SBA.Abbreviations FITC
fluorescein isothiocyanate
- IgG
immunoglobulin G
- SBA
soybean agglutinin |
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Keywords: | Glycine max (lectin) Hemagglutinating proteins Soybean agglutinin Soybean cultivars |
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