Structure and function of platelet glycoprotein Ib: study of the functional domain of glycoprotein Ib for von Willebrand factor binding using granulocyte elastase-like proteinase.
作者： Masashi Taki
DOI: 10.2302/KJM.37.37
关键词:
摘要: The structure of platelet glycoprotein Ib (GP Ib) and its functional domain for human von Willebrand factor (vWF) were investigated using an elastase-like proteinase (ELP) purified from granulocytes a monoclonal antibody (56-2) against GP which completely inhibited the interaction platelets with vWF. Treatment ELP resulted in loss their ability to interact vWF presence ristocetin. A fluorogram SDS-PAGE 3H-labelled treated revealed that band corresponding was clearly decreased fragments molecular weights (MW) 97 kilo-daltons (KD), 70 KD, 60, 47 44 37 25 KD 15 released platelets. fragment initially cleaved platelets, showed much fainter when compared fragments. Similar results obtained partially digested by ELP. When these reacted 56-2 antibody, MW immunoisolated. electrophoretic mobility three bands slightly slow under reduced conditions non-reduced conditions. should be derived since have epitope antibody. suggest binding may located less glycosylated on distal portion Ib, contain loop region at least one intramolecular disulfide bond, this important
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