Precipitation of galactose-specific lectins by complex-type oligosaccharides and glycopeptides: studies with lectins from Ricinus communis (agglutinin I), Erythrina indica, Erythrina arborescens, Abrus precatorius (agglutinin), and Glycine max (soybean)
- 1 February 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (3) , 1034-1041
- https://doi.org/10.1021/bi00403a028
Abstract
We have recently demonstrated that certain oligomannose and bisected hybrid type glycopeptides and bisected complex type oligosaccharides are bivalent for binding to concanavalin A and can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., and Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L. Haraldsson, M., and Brewer, C. F. (1987) J. Biol. Chem. 262, 1294-1299]. The present results show that tri- and tetraantennary complex type oligosaccharides containing nonreducing terminal galactose residues, and a related triantennary glycopeptide, precipitate the D-galactose-specific lectins from Ricinus communis (agglutinin I) (RCA-I), Erythrina indica (EIL), Erythrina arborescens (EAL), and Glycine max (soybean) (SBA). Nonbisected and bisected biantennary complex type oligosaccharides can precipitate SBA, which is a tetrameric lectin, but not RCA-I, EIL, or EAL, which are dimeric lectins. The relative affinities of the oligosaccharides and glycopeptides were determined by hemagglutination inhibition measurements and their valencies by quantitative precipitin analyses. The equivalence points of the precipitin curves indicate that the tri- and tetraantennary oligosaccharides are tri- and tetravalent, respectively, for EIL, EAL, and SBA binding. However, the oligosaccharides are all trivalent for RCA-I binding due apparently to the larger size of the monomeric subunit of the lectin. The triantennary glycopeptide was also trivalent for RCA-I and EIL binding. Biantennary oligosaccharides with adequate chain lengths were found to be bivalent for binding to SBA; those with shorter chains did not precipitate the lectin. The results indicate that, in general, each arm of the branched-chain oligosaccharides can bind individual lectin molecules, which leads to cross-linking and precipitation. The extent of precipitation is dependent not only on the valency of the oligosaccharides but, as in the case of the triantennary carbohydrates, on their branching patterns as well. These findings are discussed in terms of the possible structure-function properties of lectins and complex-type oligosaccharides.This publication has 27 references indexed in Scilit:
- Isolation, Physicochemical Characterization, and Carbohydrate-Binding Specificity of LectinsPublished by Elsevier ,1986
- Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides.Journal of Biological Chemistry, 1979
- Mechanism of binding of mono- and oligosaccharides to concanavalin A: a solvent proton magnetic relaxation dispersion studyBiochemistry, 1979
- Structural studies on the carbohydrate portion of fetuin.Journal of Biological Chemistry, 1979
- Soybean agglutinin–a plant glycoprotein. Structure of the carboxydrate unit.Journal of Biological Chemistry, 1978
- Isolation, purification and some properties of a lectin and abrin from Abrus precatorius linnArchives of Biochemistry and Biophysics, 1976
- Trans-membrane control of the receptors on normal and tumor cells II. Surface changes associated with transformation and malignancyBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1976
- PROTEIN-CARBOHYDRATE INTERACTION .13. INTERACTION OF CONCANAVALIN A WITH ALPHA-MANNANS FROM A VARIETY OF MICROORGANISMS1968
- Protein-Carbohydrate interactionArchives of Biochemistry and Biophysics, 1968
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964