PMID: 3755619Sep 4, 1986Paper

Structural and conformational features that affect the interaction of polylactosaminoglycans with immobilized wheat germ agglutinin

Biochimica Et Biophysica Acta
R J IvattG F Clark

Abstract

We examined the interaction between immobilized wheat germ agglutinin and the large, polylactosamine-containing glycans from human erythrocytes and human K-562 erythroleukemic cells. Three classes of interaction were identified. One class of glycan was merely retarded during chromatography. The other two classes were retained and could be distinguished by their ease of displacement with N-acetylglucosamine (GlcNAc); one was a moderate-affinity fraction displaced by 0.1 M GlcNAc and the other was a high-affinity fraction subsequently displaced by 1.0 M GlcNAc. A relatively small fraction of the K-562 polylactosamines were in the high-affinity class. We explored the role that fucose and sialic acid substitutions play in the strength of the lectin-glycan interaction. Although sialic acid is recognized by wheat germ agglutinin, sialylation was not required for the high-affinity interaction, and the presence of sialic acids actually prevented some glycans from binding with high affinity. In contrast, fucose is not part of the binding determinant, yet the removal of fucose resulted in decreased affinity. The possibility that some of these changes in affinity were the result of conformational changes was explored using matrices that h...Continue Reading

References

Oct 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·S J TurcoP W Robbins
Mar 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·M MonsignyC Hélène
Aug 15, 2002·Proceedings of the National Academy of Sciences of the United States of America·Ralph S HamesAndre A Dhondt
May 9, 2012·Journal of the American Chemical Society·Teresa E RossonSandra J Rosenthal

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