PMID: 6171254Mar 1, 1981Paper

Concanavalin A, a receptor protein with apparently co-operative binding characteristics

The Biochemical Journal
E KöttgenW Gerok

Abstract

Laser nephelometry is a suitable technique for the quantitative determination and differentiation of both lectins and glycoconjugates in the low-picomolar range. Simultaneously this method renders possible investigations on the specificity and mode of interaction between lectins and different ligands. The results demonstrate that the degree of co-operativity between concanavalin A and the respective glycoconjugate is dependent on the presence of hydrophobic binding sites and can be substantially altered by conformational changes of the ligand. The transition from apotransferrin to Fe3+-transferrin induces a transformation of the sigmoidal-shaped binding curve to a hyperbolic one. Hence, at low concentrations, Fe3+-transferrin is bound far better than apotransferrin, whereas maximal binding is nearly identical. After removal of N-acetylneuraminate, concanavalin A is less efficient in differentiating between the Fe3+-charged and Fe3+-free (apo) forms of transferrin.

Citations

Jun 3, 2014·New Journal of Chemistry = Nouveau Journal De Chimie·Yih Horng TanKeith J Stine
Feb 1, 1989·Archives of Biochemistry and Biophysics·E RegoecziP A Chindemi
Nov 16, 1982·Biochemical and Biophysical Research Communications·E KöttgenW Gerok

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