Thermodynamic parameters of the interaction of Urtica dioica agglutinin with N-acetylglucosamine and its oligomers.

Abstract:

:The interaction between Urtica dioica agglutinin (UDA) and N-acetylglucosamine (GlcNAc) and its beta(1-4)-linked oligomers was studied by fluorescence titration and isothermal titration microcalorimetry. UDA possesses one significant binding site that can be measured calorimetrically. This site is composed of three subsites, each subsite accommodating one GlcNAc residue. The interaction is enthalpically driven, and the binding area of UDA is characterized by a deltaH of interaction for a given oligosaccharide considerably smaller than that of wheat germ agglutinin (WGA), despite the fact that they both belong to a family of proteins composed entirely of hevein domains. Relatively high deltaCp values of the UDA-carbohydrate interactions and more favorable entropy term compared to WGA suggest that binding of the carbohydrate ligands by UDA has a higher hydrophobic component than that of WGA.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Lee RT,Gabius HJ,Lee YC

doi

10.1023/a:1006976129458

subject

Has Abstract

pub_date

1998-07-01 00:00:00

pages

649-55

issue

7

eissn

0282-0080

issn

1573-4986

journal_volume

15

pub_type

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