Characterization of human platelet GMP-140 as a heparin-binding protein.
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.
Skinner
M P
MP
Research Centre for Thrombosis and Cardiovascular Disease, Department of Medicine, Westmead Hospital, N.S.W., Australia.
Fournier
D J
DJ
Andrews
R K
RK
Gorman
J J
JJ
Chesterman
C N
CN
Berndt
M C
MC
D000911:Antibodies, Monoclonal; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000097:blood*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D019007:P-Selectin; D010980:Platelet Membrane Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
D000911:Antibodies, Monoclonal; D019007:P-Selectin; D010980:Platelet Membrane Glycoproteins; D006493:Heparin