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Binding and functional properties of concanavalin-a and its derivatives .3. Interactions with indoleacetic-acid and other hydrophobic ligands

Academic Article
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Overview

authors

  • Edelman, Gerald
  • Wang, J. L.

publication date

  • 1978

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The binding of concanavalin A to various structures via hydrophobic interactions has been studied using a variety of physicochemical assays. It was found that concanavalin A binds to nonpolar compounds such as the plant auxin beta-indoleacetic acid and its structural analogue tryptophan and that this binding is independent of the saccharide-binding activity normally associated with the lectin. The results of equilibrium dialysis experiments on the binding of beta-indoleacetic acid were consistent with the presence of a single weak binding site per subunit of protein, having an association constant of about 7 X 10(2) M-1. Competition experiments using various nonpolar compounds such as o-iodobenzoic acid suggested that this hydrophobic binding site is located in the same cavity which binds the iodine-containing ligand as shown by x-ray crystallography. Concanavalin A also binds to lipid vesicles composed of dipalmitoylphosphatidylcholine or 12-O-tetradecanoyl phorbol-13-O-acetate. This binding to lipid membranes raises the possibility that the synergistic effects of concanavalin A and tetradecanoyl phorbol acetate on lymphocyte mitogenesis may be due in part to an interaction between lectin and the phorbol ester.

subject areas

  • Concanavalin A
  • Indoleacetic Acids
  • Lectins
  • Ligands
  • Protein Binding
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 641053
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Additional Document Info

start page

  • 3016

end page

  • 3022

volume

  • 253

issue

  • 9

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