Isolation of the membrane glycoproteins of human blood platelets by lectin affinity chromatography.
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.
D001792:Blood Platelets / Q000032:analysis*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000097:blood / Q000302:isolation & purification; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000097:blood / Q000302:isolation & purification; D013045:Species Specificity
D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins