3.4.21.27	?	x * 160000, SDS-PAGE	36532	
3.4.21.27	?	x * 80000, SDS-PAGE	754516	
3.4.21.27	dimer	2 * 73210, FXI, SDS-PAGE	667620	
3.4.21.27	dimer	2 * 80000, recombinant mutant C362S/C482S , SDS-PAGE	683160	
3.4.21.27	dimer	2 * 80000, SDS-PAGE	669347	
3.4.21.27	dimer	the dimer is required for normal function in vivo	732936	
3.4.21.27	dimer	two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX	683682	
3.4.21.27	homodimer	2 * 68000, SDS-PAGE	732897	
3.4.21.27	homodimer	2 * 80000	709721, 709722, 718042	
3.4.21.27	homodimer	2 * 80000, SDS-PAGE	669420	
3.4.21.27	monomer	1 * 72626, mutant FXI/G326C, SDS-PAGE	667620	
3.4.21.27	monomer	1 * 79600, SDS-PAGE	36541	
3.4.21.27	additional information	macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa are required for mediation of formation of the Michaelis complex required for factor IX-activation, overview	683167	
3.4.21.27	polymer	x * 35000, x * 48000, SDS-PAGE, 2 chains	36532