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Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential by David Gailani, David Ho, Mao-Fu Sun, Qiufang Cheng, and Peter N. Walsh Blood Volume 97(10):3117-3122 May 15, 2001 ©2001 by American Society of Hematology SDS-PAGE and size-exclusion chromatography of plasma-derived and recombinant proteins.(A) SDS-polyacrylamide gel of proteins stained with Gelcode Blue. David Gailani et al. Blood 2001;97:3117-3122 ©2001 by American Society of Hematology Binding of FXI and chimeric proteins to activated platelets.FXI and FXI/PK chimeras were used in competition binding studies as competitive ligands for 22 nM 125I-FXI binding to activated platelets in the presence of 50 nM HK and 25 μM ZnCl2. David Gailani et al. Blood 2001;97:3117-3122 ©2001 by American Society of Hematology Western immunoblot analysis of factor IX activation by FXIa in the presence of platelets.(A) Factor IX (150 nM) was incubated with 1 nM wild-type FXIa or activated FXI/PKA4 in TBSA containing 2 mM CaCl2. David Gailani et al. Blood 2001;97:3117-3122 ©2001 by American Society of Hematology A model for the activation of FXI and factor IX on activated platelets.The FXI or FXIa molecule is a dimer composed of 2 identical 80-kd polypeptides, each containing 4 apple domains (designated A1 through A4), and one trypsin-like catalytic domain. David Gailani et al. Blood 2001;97:3117-3122 ©2001 by American Society of Hematology