A surface plasmon resonance assay for the binding of Amaranthus hypochondriacus var. Mexico lectin to glycoprotein

Biochem Mol Biol Int. 1998 Jan;44(1):211-6. doi: 10.1080/15216549800201232.

Abstract

We have used the analytical system based on surface plasmon resonance to monitor the interaction between Amaranthus hypochondriacus var. Mexico lectin and four different fetuins; fetuin, asialofetuin, agalactofetuin, and agalactosaminofetuin. Agalactofetuin and agalactosaminofetuin were prepared by enzymic digestion of asialofetuin using jack bean beta-galactosidase or endo-alpha-N-acetylgalactosaminidase from Diplococcus pneumoniae. Ligands were immobilized onto a sensor surface via amide linkages. The lectin interacted most strongly with asialofetuin, but not with agalactosaminofetuin. The binding of the lectin to asialofetuin was inhibited by N-acetylgalactosamine or Gal beta 1-->3GalNAc in a dose-dependent manner.

MeSH terms

  • Asialoglycoproteins / metabolism
  • Binding, Competitive / drug effects
  • Biosensing Techniques*
  • Fetuins
  • Glycoproteins / metabolism*
  • Lectins / metabolism*
  • Plant Proteins / metabolism*
  • Protein Binding / drug effects
  • alpha-Fetoproteins / metabolism*

Substances

  • Asialoglycoproteins
  • Fetuins
  • Glycoproteins
  • Lectins
  • Plant Proteins
  • alpha-Fetoproteins
  • asialofetuin