Characterization of human platelet GMP-140 as a heparin-binding protein

Biochem Biophys Res Commun. 1989 Nov 15;164(3):1373-9. doi: 10.1016/0006-291x(89)91821-4.

Abstract

Human platelet GMP-140 has been identified as a heparin-binding protein. Purified platelet GMP-140 bound to Heparin-Sepharose CL-6B and was eluted by approximately 0.5 M sodium chloride. Radioiodinated GMP-140 bound specifically and saturably to heparin immobilized on Matrex-Pel 102 beads. Binding of radioiodinated GMP-140 to heparin-Matrex-Pel 102 beads was divalent cation-independent and was strongly inhibited by excess fluid phase GMP-140 and heparin and by other sulfated glycans such as fucoidin and dextran-sulfate. Binding was not inhibited by chondroitins 4- and 6-sulfate or mannose 6-phosphate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Cell Membrane / metabolism
  • Chromatography, Affinity
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Heparin / blood*
  • Humans
  • Kinetics
  • Molecular Weight
  • P-Selectin
  • Platelet Membrane Glycoproteins / isolation & purification
  • Platelet Membrane Glycoproteins / metabolism*
  • Protein Binding

Substances

  • Antibodies, Monoclonal
  • P-Selectin
  • Platelet Membrane Glycoproteins
  • Heparin