PMID: 6165390Apr 22, 1981Paper

Interaction of monolayers of concanavalin A with mono- and polysaccharides. A study by means of infrared-attenuated total reflectance spectroscopy

Biochimica Et Biophysica Acta
N Ockman

Abstract

The effects of pH, Mn2+ and Ca2+ and urea denaturation on the interaction of monolayers of concanavalin A on saline with the polysaccharide dextran B-1355 and the monosaccharides methyl alpha-D-mannopyranoside and D-galactose have been investigated. Infrared absorption spectra of compressed monolayers of the protein and the protein-dextran complex coated on a germanium plate have been obtained by means of attenuated total reflectance spectroscopy. Except in one case of denaturation, the amide I absorption of concanavalin A peaked around 1631 cm-1, indicating a predominance of the beta-pleated sheet conformation, in agreement with its secondary structure in the solution and crystalline phases. The contribution to the absorbance of the concanavalin A-dextran films at 3300 cm-1 due to absorption by the O-H stretching modes of the polysaccharide is a measure of its binding. Increasing the pH from 6.1 to 7.5 appreciably reduced the dextran binding, at pH 9.3 the binding was zero. Adding 1 mM Mn2+ and Ca2+ to the subphase at pH 7.5 restored both the dextran binding and the affinity of concanavalin A for methyl alpha-D-mannopyranoside to that of the native protein at pH 6.1. At this latter pH, the weak binding of dextran to monolayers...Continue Reading

References

Jan 1, 1978·Advances in Protein Chemistry·F Macritchie
Oct 17, 1977·Biochimica Et Biophysica Acta·B D ReadL L van Deenen
Jan 1, 1975·Advances in Experimental Medicine and Biology·I J Goldstein
Nov 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·M InbarL Sachs
Nov 19, 1974·Biochemistry·M N Pflumm, S Beychok
Aug 9, 1972·Biochimica Et Biophysica Acta·I VlodavskyL Sachs

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