TY - JOUR
T1 - Binding and precipitation of lectins from Erythrina indica and Ricinus communis (Agglutinin I) with synthetic cluster glycosides
AU - Bhattacharyya, Lokesh
AU - Brewer, C. Fred
N1 - Funding Information:
ACKNOWLEDGMENTS The authors thank Drs. R. T. Lee and Y. C. Lee, The Johns Hopkins University, Baltimore, Maryland, for the generous gift of the cluster glycosides. This work was supported by Grant CA-16054 from the National Cancer Institute, Department of Health, Education, and Welfare, and Core Grant P30 CA-13330 from the. same agency.
PY - 1988/5/1
Y1 - 1988/5/1
N2 - We recently reported that tri- and tetraantennary complex type oligosaccharides with nonreducing terminal galactose residues and the triantennary asialofetuin glycopeptide can bind and precipitate certain galactose specific lectins (L. Bhattacharyya, and C. F. Brewer (1986) Biochem. Biophys. Res. Commun., 141, 963-967; L. Bhattacharyya, M. Haraldsson, and C. F. Brewer (1988) Biochemistry 27,1034-1041). The present study investigates the binding interactions of two of these lectins, those from Erythrina indica and Ricimis communis (Agglutinin I), with mono-, bi-, and triantennary synthetic cluster glycosides, which have little structural resemblance to complex type oligosaccharides other than they possess nonreducing terminal galactose residues (R. T. Lee, P. Lin, and Y. C. Lee (1984) Biochemistry 23, 4255-4261). The enhanced affinities of the bi-and triantennary glycosides relative to the monoantennary glycoside for the two lectins are consistent with an increase in the probability of binding due to multiple binding residues in the multiantennary glycosides. The triantennary glycoside is capable of precipitating the two lectins, and quantitative precipitation data indicate that it is a tri-valent ligand. The results show that the binding and precipitation activities of complex type oligosaccharides with these lectins is due solely to the presence of multiple terminal galactose residues and not to the overall structures of the oligosaccharides.
AB - We recently reported that tri- and tetraantennary complex type oligosaccharides with nonreducing terminal galactose residues and the triantennary asialofetuin glycopeptide can bind and precipitate certain galactose specific lectins (L. Bhattacharyya, and C. F. Brewer (1986) Biochem. Biophys. Res. Commun., 141, 963-967; L. Bhattacharyya, M. Haraldsson, and C. F. Brewer (1988) Biochemistry 27,1034-1041). The present study investigates the binding interactions of two of these lectins, those from Erythrina indica and Ricimis communis (Agglutinin I), with mono-, bi-, and triantennary synthetic cluster glycosides, which have little structural resemblance to complex type oligosaccharides other than they possess nonreducing terminal galactose residues (R. T. Lee, P. Lin, and Y. C. Lee (1984) Biochemistry 23, 4255-4261). The enhanced affinities of the bi-and triantennary glycosides relative to the monoantennary glycoside for the two lectins are consistent with an increase in the probability of binding due to multiple binding residues in the multiantennary glycosides. The triantennary glycoside is capable of precipitating the two lectins, and quantitative precipitation data indicate that it is a tri-valent ligand. The results show that the binding and precipitation activities of complex type oligosaccharides with these lectins is due solely to the presence of multiple terminal galactose residues and not to the overall structures of the oligosaccharides.
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U2 - 10.1016/0003-9861(88)90412-2
DO - 10.1016/0003-9861(88)90412-2
M3 - Article
C2 - 3364983
AN - SCOPUS:0024003044
SN - 0003-9861
VL - 262
SP - 605
EP - 608
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -