Isolation of the Membrane Glycoproteins of Human Blood Platelets by Lectin Affinity Chromatography

Biochim Biophys Acta. 1977 Feb 4;464(3):493-508. doi: 10.1016/0005-2736(77)90025-6.

Abstract

The major platelet membrane glycoproteins have been solubilized in 1.0% sodium deoxycholate and subjected to affinity chromatography on the lectins from Lens culinaris, wheat germ and Abrus precatorius. Polyacrylamide gel electrophoresis in the presence and absence of a reducing agent together with the differential binding of the lectins to the glycoproteins permitted the distinction of at least seven separate glycoprotein entities. A new nomenclature for the glycoproteins is proposed to accomodate the additional data. Using combinations of lectin columns, glycoproteins Ia and Ib could be prepared in a pure state and IIb and IIIa could be greatly purified. The binding of lectins to glycoprotein Ib has been strongly implicated as a necessary step in the aggregation response of platelets to lectins.

MeSH terms

  • Blood Platelets / analysis*
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins* / blood
  • Glycoproteins* / isolation & purification
  • Humans
  • Lectins
  • Membrane Proteins* / blood
  • Membrane Proteins* / isolation & purification
  • Species Specificity

Substances

  • Glycoproteins
  • Lectins
  • Membrane Proteins