Isolation of the membrane glycoproteins of human blood platelets by lectin affinity chromatography
KJ Clemetson, SL Pfueller, EF Luscher… - Biochimica et Biophysica …, 1977 - Elsevier
KJ Clemetson, SL Pfueller, EF Luscher, CSP Jenkins
Biochimica et Biophysica Acta (BBA)-Biomembranes, 1977•ElsevierThe 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 …
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 …
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.
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