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)

Lokesh Bhattacharyya, Martin Haraldsson, Curtis F. Brewer

Research output: Contribution to journalArticle

81 Citations (Scopus)

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., & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., & 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 glycopeptide 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.

Original languageEnglish (US)
Pages (from-to)1034-1041
Number of pages8
JournalBiochemistry
Volume27
Issue number3
StatePublished - 1988

Fingerprint

Abrus
Erythrina
Glycopeptides
Oligosaccharides
Galactose
Soybeans
Lectins
Glycine
Precipitates
Precipitins
Branched-Chain Oligosaccharides
abrus agglutinin
Ricinus communis agglutinin-1
Hemagglutination
Concanavalin A
Chain length
Carbohydrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{cfddaee289eb41c084b38e8d1b19b9bd,
title = "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)",
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., & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., & 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 glycopeptide 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.",
author = "Lokesh Bhattacharyya and Martin Haraldsson and Brewer, {Curtis F.}",
year = "1988",
language = "English (US)",
volume = "27",
pages = "1034--1041",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - Precipitation of galactose-specific lectins by complex-type oligosaccharides and glycopeptides

T2 - Studies with lectins from Ricinus communis (agglutinin I), Erythrina indica, Erythrina arborescens, Abrus precatorius (agglutinin), and Glycine max (soybean)

AU - Bhattacharyya, Lokesh

AU - Haraldsson, Martin

AU - Brewer, Curtis F.

PY - 1988

Y1 - 1988

N2 - 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., & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., & 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 glycopeptide 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.

AB - 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., & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., & 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 glycopeptide 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.

UR - http://www.scopus.com/inward/record.url?scp=0024282305&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024282305&partnerID=8YFLogxK

M3 - Article

VL - 27

SP - 1034

EP - 1041

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 3

ER -