PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10089894-0	1999	Selectivity of von Willebrand factor triplet bands towards heparin binding supports structural model.	Heparin	59-66	von Willebrand factor	Homo sapiens	15-36	
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	52-55	
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105	
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105	
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105	
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105	
10089894-4	1999	By contrast, faster migrating satellite bands and slower migrating satellite bands of hp-vWF exhibited reduced and increased heparin affinity, respectively, compared to the intermediate band of the same triplet.	Heparin	125-132	von Willebrand factor	Homo sapiens	89-92	
10089894-5	1999	Because heparin binding sites are localised in the N-terminal domain of the hp-vWF subunit, this result confirms a structural model of hp-vWF (Fischer et al., Biochem.	Heparin	8-15	von Willebrand factor	Homo sapiens	79-82