A radioaffinity assay for lectin binding to receptors was developed and characterized by using the interactions between soya-bean agglutinin and four glycoconjugates, namely thyroglobulin, galactomannan, fetuin and asialofetuin. On application of the assay to soya-bean extracts a wide range of seed components were found to have the capacity to interact with soya-bean agglutinin. These included both trichloroacetic acid-soluble and trichloroacetic acid-insoluble glycoconjugates and two classes of particulate matter distinguished by their differential solubility in Triton X-100.
Research Article|May 15 1985
Interactions of soya-bean agglutinin with purified glycoconjugates and soya-bean seed components
Biochem J (1985) 228 (1): 127-136.
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H M Bond, M F Chaplin, D J Bowles; Interactions of soya-bean agglutinin with purified glycoconjugates and soya-bean seed components. Biochem J 15 May 1985; 228 (1): 127–136. doi: https://doi.org/10.1042/bj2280127
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