-transparent.png){kind=logo}
We describe the synthesis of N-trifluoroacetyl chito-oligosaccharides and their use as ligands to probe the binding sites of wheat-germ agglutinin, a lectin specific for N-acetylglucosamine. The binding is monitored using intrinsic protein fluorescence, which is due to tryptophan side-chains. We present arguments purporting to show the presence of a fluorophore close to each of the four sites. The binding of chito-oligosaccharides to wheat-germ agglutinin is complex and can only be approximately described by an independent and equivalent sites model. This model applies when the ligand concentration range is restricted to higher values. The possible role of ligand-mediated protein aggregation and of site inequivalence is discussed. We find that the affinity of trifluoroacetylated chito-oligosaccharides for wheat-germ agglutinin is higher than that of the N-acetylated parent compounds, the difference increasing with chain length. Our results are in agreement with a model of the binding site previously proposed by Clegg et al. (Biochemistry 22 (1983) 4797-4804).
P Gatellier, and
J P Grivet, and
F Delmotte
October 1980,
FEBS letters,
P Gatellier, and
J P Grivet, and
F Delmotte
August 1974,
European journal of biochemistry,
P Gatellier, and
J P Grivet, and
F Delmotte
October 2009,
Cytometry. Part A : the journal of the International Society for Analytical Cytology,
P Gatellier, and
J P Grivet, and
F Delmotte
March 1984,
Biochemical and biophysical research communications,
P Gatellier, and
J P Grivet, and
F Delmotte
September 1981,
Biochemistry,
P Gatellier, and
J P Grivet, and
F Delmotte
May 2004,
Biochimica et biophysica acta,
P Gatellier, and
J P Grivet, and
F Delmotte
July 1980,
Biochemical and biophysical research communications,
P Gatellier, and
J P Grivet, and
F Delmotte
February 1973,
Nature: New biology,
P Gatellier, and
J P Grivet, and
F Delmotte
October 1985,
The Biochemical journal,
P Gatellier, and
J P Grivet, and
F Delmotte
December 1992,
Biochemistry,
