PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10605949-2	1999	We examined the effect of vWF on kinetic parameters for interaction between LCh and HCh in the presence of Ca2+ and Mn2+ ions, the most effective mediators of fVIII reconstitution from isolated subunits, and determined the minimal structural portion of vWF able to enhance fVIII formation.	alpha-hexachlorocyclohexane	84-87	von Willebrand factor	Homo sapiens	26-29	
10605949-3	1999	We found that affinity (Kd) for LCh/HCh binding mediated by Ca2+ and Mn2+ was 91 and 34.9 nM in the absence of vWF and 15.5 and 5.6 nM in its presence.	alpha-hexachlorocyclohexane	36-39	von Willebrand factor	Homo sapiens	111-114	
10605949-5	1999	The value of the dissociation rate constant (k(off)) for LCh/HCh complex was lower in the presence of Mn2+ (k(off) 4.6x 10(-6) s(-1)) than Ca2+ (k(off) 8.4 x 10(-6) s(-1)) but in both cases vWF had no effect on k(off).	alpha-hexachlorocyclohexane	61-64	von Willebrand factor	Homo sapiens	190-193	
10605949-9	1999	Only vWF large proteolytic N-terminal homodimeric fragment SPIII (vWF residues 1-1365), but not small monomeric N-terminal fragment SPIII-T4 (1-272), both of which are known to contain a major fVIII binding site, was able to support reconstitution of fVIII activity from isolated LCh and HCh subunits in the presence of Mn2+ or Ca2+.	alpha-hexachlorocyclohexane	288-291	von Willebrand factor	Homo sapiens	5-8	
10480230-6	1999	The finding that Kd of LCh binding to vWf (3.8 nM) is 9.5 times higher than that of fVIII (0.4 nM), indicates that the heavy chain (HCh) is required for the maximal affinity of fVIII for vWf.	alpha-hexachlorocyclohexane	132-135	von Willebrand factor	Homo sapiens	38-41	
10480230-6	1999	The finding that Kd of LCh binding to vWf (3.8 nM) is 9.5 times higher than that of fVIII (0.4 nM), indicates that the heavy chain (HCh) is required for the maximal affinity of fVIII for vWf.	alpha-hexachlorocyclohexane	132-135	von Willebrand factor	Homo sapiens	187-190