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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