TY - JOUR
T1 - Characterization of human platelet GMP-140 as a heparin-binding protein
AU - Skinner, Michael P.
AU - Fournier, Dominique J.
AU - Andrews, Robert K.
AU - Gorman, Jeffrey J.
AU - Chesterman, Colin N.
AU - Berndt, Michael C.
PY - 1989/11/15
Y1 - 1989/11/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024425385&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(89)91821-4
DO - 10.1016/0006-291X(89)91821-4
M3 - Article
C2 - 2480118
AN - SCOPUS:0024425385
VL - 164
SP - 1373
EP - 1379
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -