Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin

M. Islam Khan, Dipak K. Mandal, Curtis F. Brewer

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C. F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA.

Original languageEnglish (US)
Pages (from-to)69-77
Number of pages9
JournalCarbohydrate Research
Volume213
Issue numberC
DOIs
StatePublished - Jun 25 1991

Fingerprint

Concanavalin A
Glycoproteins
Glycopeptides
Oligosaccharides
Biochemistry
Soybeans
Lectins
soybean lectin
Proteins
Monomers
Carbohydrates
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry

Cite this

Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin. / Islam Khan, M.; Mandal, Dipak K.; Brewer, Curtis F.

In: Carbohydrate Research, Vol. 213, No. C, 25.06.1991, p. 69-77.

Research output: Contribution to journalArticle

@article{97cae57294ff4c31bf9a3c8880089e01,
title = "Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin",
abstract = "Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C. F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA.",
author = "{Islam Khan}, M. and Mandal, {Dipak K.} and Brewer, {Curtis F.}",
year = "1991",
month = "6",
day = "25",
doi = "10.1016/S0008-6215(00)90599-8",
language = "English (US)",
volume = "213",
pages = "69--77",
journal = "Carbohydrate Research",
issn = "0008-6215",
publisher = "Elsevier BV",
number = "C",

}

TY - JOUR

T1 - Interactions of concanavalin A with glycoproteins. A quantitative precipitation study of concanavalin A with the soybean agglutinin

AU - Islam Khan, M.

AU - Mandal, Dipak K.

AU - Brewer, Curtis F.

PY - 1991/6/25

Y1 - 1991/6/25

N2 - Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C. F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA.

AB - Certain oligomannose-type glycopeptides have been previously shown to be bivalent for binding to concanavalin A and capable of precipitating the lectin by forming homogeneous cross-linked lattices [L. Bhattacharyya, M. I. Khan, and C. F. Brewer, Biochemistry, 27 (1988) 8762-8767]. In the present study, the effect of protein environment on the binding properties of an oligomannose-type oligosaccharide has been examined through quantitative precipitation analysis of the interactions of concanavalin A (Con A) with the soybean (Glycine max) agglutinin (SBA), which is a tetrameric glycoprotein possessing a single Man9-oligomannose chain per monomer. The results showed that SBA forms two different types of cross-linked complexes with tetrameric Con A, depending on the relative ratio of the two molecules in solution. At a concentration of one equivalent or less, SBA forms a 1:1 complex with Con A. At concentrations exceeding one equivalent, SBA forms a 2:1 complex with Con A. However, SBA forms only 1:1 cross-linked complexes with dimeric forms of Con A, such as acetyl- and succinyl-Con A. The results demonstrated that the total valency of the carbohydrate of SBA is a function of both the quaternary structure of Con A, as well as the relative ratio of SBA to Con A. In addition, the individual Man9-oligosaccharide, which as a glycopeptide is bivalent for binding to Con A, expresses univalency when present on the protein matrix of SBA.

UR - http://www.scopus.com/inward/record.url?scp=0026174247&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026174247&partnerID=8YFLogxK

U2 - 10.1016/S0008-6215(00)90599-8

DO - 10.1016/S0008-6215(00)90599-8

M3 - Article

C2 - 1933954

AN - SCOPUS:0026174247

VL - 213

SP - 69

EP - 77

JO - Carbohydrate Research

JF - Carbohydrate Research

SN - 0008-6215

IS - C

ER -