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 ∼0.5 M sodium chloride. Radioiodinated GMP-140 bound specifically and saturably to heparin immobilized on Matrex-Pel 102 beads. Binding of radioiodina...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1989-11, Vol.164 (3), p.1373-1379 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Skinner, Michael P. Fournier, Dominique J. Andrews, Robert K. Gorman, Jeffrey J. Chesterman, Colin N. Berndt, Michael C. |
| description | 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 ∼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. |
| doi_str_mv | 10.1016/0006-291X(89)91821-4 |
| format | Article |
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Purified platelet GMP-140 bound to Heparin-Sepharose CL-6B and was eluted by ∼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. 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Purified platelet GMP-140 bound to Heparin-Sepharose CL-6B and was eluted by ∼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.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Heparin - blood</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>P-Selectin</subject><subject>Platelet Membrane Glycoproteins - isolation & purification</subject><subject>Platelet Membrane Glycoproteins - metabolism</subject><subject>platelets</subject><subject>Protein Binding</subject><subject>Proteins</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFuEzEQhq0KVELpGxRpDwjBYWHG63XWl0ooakOlIjiAxM2a9c42RhtvsDeVytPjNFGO7cW2NN_8M_6EuED4hID6MwDoUhr8_aExHw02Ekt1ImYIBkqJoF6I2RF5JV6n9AcAUWlzKk6lavK7mYnlYkWR3MTR_6PJj6EY-2K1XVMoNgNNPPBULL_9KFFBQamgYsUbij6UrQ-dD3fFJo4T-_BGvOxpSHx-uM_Er-urn4uv5e335c3iy23pVFNN-XRt3xvJ2NZzU7XSkDJAmgENtNQ42SHNVcugtVROOwlaKe062ebVa1mdiff73Dz375bTZNc-OR4GCjxuk82htZZV9SyItZorrCGDag-6OKYUubeb6NcUHyyC3Ym2O4t2Z9E2xj6Ktiq3vT3kb9s1d8emg9lcf3eoU3I09JGC8-mIaT3PP8aMXe4xztLuPUebnOfguPOR3WS70T-9x3_F5pee</recordid><startdate>19891115</startdate><enddate>19891115</enddate><creator>Skinner, Michael P.</creator><creator>Fournier, Dominique J.</creator><creator>Andrews, Robert K.</creator><creator>Gorman, Jeffrey J.</creator><creator>Chesterman, Colin N.</creator><creator>Berndt, Michael C.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19891115</creationdate><title>Characterization of human platelet GMP-140 as a heparin-binding protein</title><author>Skinner, Michael P. ; Fournier, Dominique J. ; Andrews, Robert K. ; Gorman, Jeffrey J. ; Chesterman, Colin N. ; Berndt, Michael C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-c4cbff92e1b5793b29a490a6e0190ba8c2d1a74be06624c6c206446cd2b114523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Antibodies, Monoclonal</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. 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| ispartof | Biochemical and biophysical research communications, 1989-11, Vol.164 (3), p.1373-1379 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Analytical, structural and metabolic biochemistry Antibodies, Monoclonal Biological and medical sciences Cell Membrane - metabolism Chromatography, Affinity Chromatography, Gel Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Glycoproteins Heparin - blood Humans Kinetics Molecular Weight P-Selectin Platelet Membrane Glycoproteins - isolation & purification Platelet Membrane Glycoproteins - metabolism platelets Protein Binding Proteins |
| title | Characterization of human platelet GMP-140 as a heparin-binding protein |
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