Conversion of low-affinity platelet factor 4 to beta-thromboglobulin by plasmin and trypsin.
Conversion of low-affinity platelet factor 4 to beta-thromboglobulin by plasmin and trypsin.
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DOI：
10.1016/0304-4165(80)90086-0
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发表时间：
1980-10
期刊：
影响因子：
--
通讯作者：
J. Holt;S. Niewiarowski
中科院分区：
文献类型：
--
作者：
J. Holt;S. Niewiarowski
Low-affinity platelet factor 4 and β-thromboglobulin are platelet-secreted proteins that bind with low affinity to heparin. They show extensive immunological cross-reactivity and appear to differ in amino acid sequence only by an amino-terminal peptide unique to low-affinity platelet factor 4. The possibility that β-thromboglobulin is derived from low-affinity platelet factor 4 by proteolysis was investigated by exposing this protein to the action of plasmin, thrombin and trypsin. While thrombin had no effect, plasmin and trypsin converted low-affinity platelet factor 4 to a species with the same electrophoretic mobility and isoelectric point as β-thromboglobulin. We conclude that β-thromboglobulin is a breakdown product of low-affinity platelet factor 4.
