Characterization of human platelet GMP-140 as a heparin-binding protein |
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Authors: | M P Skinner D J Fournier R K Andrews J J Gorman C N Chesterman M C Berndt |
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Institution: | Research Centre for Thrombosis and Cardiovascular Disease, Department of Medicine, Westmead Hospital, N.S.W., Australia. |
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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. |
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