Interactions of soya-bean agglutinin with purified glycoconjugates and soya-bean seed components

Abstract

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.

Phytate-mineral-protein composition of soybeans: gel filtration studies of soybean meal extracts

“…Associations of agglutinin with other soybean glycosides and proteins have been reported (Bond et al, 1985;Einhoffetal., 1986). Differences in the content of 1 IS protein in fractions V and VI, as determined by ultracentrifugal analyses in Tris-HCl as compared to analyses in standard buffer, suggest partial dissociation of 11S into halfmolecules in Tris-HCl buffer (Wolf and Briggs, 1958).…”