TY - JOUR
T1 - Precipitation of the D-galactose specific lectin from Erythrina indica by a triantennary complex type oligosaccharide
AU - Lokesh Bhattacharyya, C.
AU - Brewer, Fred
N1 - Funding Information:
The authors wish to thank Mr. Martin Haraldsson, Arrhenius Laboratory, University of Stockholm, Stockholm, Sweden, and Drs. 3orgen Lonngren, Pharmacia Fine Chemicals, Uppsala, Sweden, and Hans Lonn, Bio-Carb AB, Sweden, lor generous gifts of the triantennary oligosaccharide. This work was supported by Grant CA-16054, awarded to C. F. B., from the National Cancer Institute, Department of Health, Education, and Welfare, and Core Grant P30 CA-13330 from the same agency.
PY - 1986/12/30
Y1 - 1986/12/30
N2 - We have previously demonstrated that a high mannose type glycopeptide is bivalent for binding Concanavalin A (Con A) and can precipitate the lectin (Bhattacharyya L. and Brewer, C.F. (1986) Biochem. Biophys. Res. Commun. 137, 670-674). The present results show that a triantennary complex type oligosaccharide containing nonreducing terminal galactose residues can precipitate the D-galactose/Nacetyl-D-galactosamine specific lectin from Erythrina indica (EIL). The interactions of the oligosaccharide with EIL was investigated by quantitatitve precipitin analysis. The equivalence point of the precipitin curve indicated that the glycopeptide is trivalent for EIL binding. These results indicate that each arm of the oligosaccharide can independently bind separate lectin molecules leading to precipitation of the complex. These findings are discussed in terms of the possible biological structure-function properties of complex type oligosaccharides.
AB - We have previously demonstrated that a high mannose type glycopeptide is bivalent for binding Concanavalin A (Con A) and can precipitate the lectin (Bhattacharyya L. and Brewer, C.F. (1986) Biochem. Biophys. Res. Commun. 137, 670-674). The present results show that a triantennary complex type oligosaccharide containing nonreducing terminal galactose residues can precipitate the D-galactose/Nacetyl-D-galactosamine specific lectin from Erythrina indica (EIL). The interactions of the oligosaccharide with EIL was investigated by quantitatitve precipitin analysis. The equivalence point of the precipitin curve indicated that the glycopeptide is trivalent for EIL binding. These results indicate that each arm of the oligosaccharide can independently bind separate lectin molecules leading to precipitation of the complex. These findings are discussed in terms of the possible biological structure-function properties of complex type oligosaccharides.
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U2 - 10.1016/S0006-291X(86)80137-1
DO - 10.1016/S0006-291X(86)80137-1
M3 - Article
C2 - 3814128
AN - SCOPUS:0023060053
SN - 0006-291X
VL - 141
SP - 963
EP - 967
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -