Purification and characterization of a hemagglutinin from Arachis hypogeae

Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1685-92. doi: 10.1515/bchm2.1975.356.2.1685.

Abstract

A. hypogaea hemagglutinin was purified by ammonium sulfate fractionation and Sepharose 6 B column chromatography. The homogeneity of the purified hemagglutinin was ascertained by ultracentrifugal analysis and polyacrylamide gel electrophoresis. It has a molecular weight of 106.500 and is a tetramer of a subunit with a molecular weight of 27.000. The purified hemagglutinin agglutinated neuraminidase-treated human erythrocytes regardless of their ABO group type, but did not agglutinate intact erythrocytes. In hapten inhibition assays with simple sugars, the so-called Mäkelä's group 2 sugars, which bear the same configuration of hydroxy groups at C-3 and C-4 as D-galactopyranose, were inhibitors for this hemagglutinin. It does not contain any carbohydrate, in contrast to most phytohemagglutinins except concanavalin A and wheat germ agglutinin.

MeSH terms

  • ABO Blood-Group System
  • Agglutinins / analysis*
  • Amino Acids / analysis
  • Binding Sites
  • Carbohydrates / analysis
  • Cell Membrane
  • Erythrocytes
  • Glycopeptides / blood
  • Glycoproteins / blood
  • Hemagglutinins / analysis*
  • Humans
  • Macromolecular Substances
  • Molecular Weight
  • Neuraminidase
  • Protein Binding
  • Seeds / analysis*

Substances

  • ABO Blood-Group System
  • Agglutinins
  • Amino Acids
  • Carbohydrates
  • Glycopeptides
  • Glycoproteins
  • Hemagglutinins
  • Macromolecular Substances
  • Neuraminidase