PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2742875-7	1989	Whereas the starting hHDL3 ligand was free of apoE, there was a substantial (7-fold) conversion of the HDL3 to apoE-containing HDL3 following in vivo circulation of the ligand, as shown by sodium phosphotungstate-MgCl2 precipitation or heparin-Sepharose column chromatography.	Sepharose	244-253	HDL3	Homo sapiens	103-107	
16022192-1	2005	The objective of the present study was to establish whether high-density lipoprotein 3 (HDL3) or high-density lipoprotein 2 (HDL2) might show an anti-oxidative effect on the acceleration of the oxidative modification of low-density lipoprotein (LDL) by ascorbic acid from measurement of the agarose gel electrophoretic mobility of LDL.	Sepharose	291-298	HDL3	Homo sapiens	60-86	
16022192-1	2005	The objective of the present study was to establish whether high-density lipoprotein 3 (HDL3) or high-density lipoprotein 2 (HDL2) might show an anti-oxidative effect on the acceleration of the oxidative modification of low-density lipoprotein (LDL) by ascorbic acid from measurement of the agarose gel electrophoretic mobility of LDL.	Sepharose	291-298	HDL3	Homo sapiens	88-92	
8132633-4	1994	Quantitative analysis of electrophoretic mobilities in agarose gels indicates that the surface potentials of reconstituted pre-beta HDL and alpha-HDL3 are -7.6 and -11.4 mV, respectively.	Sepharose	55-62	HDL3	Homo sapiens	146-150	
1402396-10	1992	In contrast, A-I/A-II-HDL2 were twice as effective as A-I-HDL2 in liberating hepatic lipase immobilized on HDL3-Sepharose.	Sepharose	112-121	HDL3	Homo sapiens	107-111	
213426-4	1978	Using system involving Sepharose-bound HDL, it could be shown that not only free apoprotein molecules but subunits consisting of lipid-apoprotein combinations were exchanged between HDL2 and HDL3.	Sepharose	23-32	HDL3	Homo sapiens	191-195	
6809752-3	1982	The HDL3 fraction purified from the AI Milano subjects eluted as a symmetrical peak from a 6% agarose column, corresponding to a unimodal particle size distribution.	Sepharose	94-101	HDL3	Homo sapiens	4-8	
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Sepharose	103-110	HDL3	Homo sapiens	34-38	
2993464-6	1985	On agarose gel electrophoresis, pH 8.6, the nitrated HDL3 moved ahead of the control HDL3, indicating an increase in negative charges in the molecule.	Sepharose	3-10	HDL3	Homo sapiens	53-57	
7159489-6	1982	In studies with lipoproteins linked to Sepharose 4B, LCAT was found to bind LDL, HDL2, and HDL3.	Sepharose	39-48	HDL3	Homo sapiens	91-95