Structural analysis of human platelet membrane glycoprotein I complex Academic Article uri icon

Overview

MeSH Major

  • Blood Platelets
  • Glycoproteins
  • Membrane Proteins

abstract

  • The glycoprotein I complex, consisting of two polypeptides of Mr 210,000 and 150,000, was isolated from human platelet membranes by wheat germ lectin affinity chromatography. Glycocalicin, a soluble loosely bound membrane glycoprotein of Mr 150,000 related to the glycoprotein I system, was also purified. The isolated polypeptides were radioiodinated in sodium dodecyl sulfate/polyacrylamide gels and digested with trypsin, and the labeled peptide digest was analyzed by two-dimensional high-voltage electrophoresis and thin-layer chromatography. The two polypeptides of Mr 210,000 and 150,000 in the glycoprotein I complex had essentially identical radioactive peptide maps. Glycocalicin had a completely different tryptic peptide map. These studies shed light on the molecular relationships of some of the components of the platelet membrane glycoprotein I system. The possibility is raised that the receptorlike function of the intrinsic platelet membrane glycoproteins may be related to the polymeric subunit associations of the constituent polypeptides.

publication date

  • December 1979

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC383728

PubMed ID

  • 288080

Additional Document Info

start page

  • 2952

end page

  • 4

volume

  • 76

number

  • 6