PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6300064-3	1983	Fractionation of the extracts by DEAE-cellulose and Sephadex G-150 chromatography yielded a purified actin that would copolymerize with rabbit skeletal muscle actin or polymerize alone into long filaments at 24 degrees C upon addition of 100 mM KC1 and 2 mM MgCl2.	sephadex	52-66	actin	Oryctolagus cuniculus	101-106	
135724-4	1976	Analysis of crude actin extract before and after precipitation by antiserum (i) by Sephadex G-200 chromatography and (ii) for its stimulating effect on myosin ATPase activity showed that actin was selectively removed.	sephadex	83-97	actin	Oryctolagus cuniculus	18-23	
6893042-3	1980	More than 80% of the actin in this supernate was found to be monomeric upon gel filtration chromatography through a Sephadex G-150 column or by a DNase I inhibition assay.	sephadex	116-130	actin	Oryctolagus cuniculus	21-26	
6893042-5	1980	Actin was purified to near homogeneity from the Sephadex G-150 pool with high yield.	sephadex	48-62	actin	Oryctolagus cuniculus	0-5	
135724-4	1976	Analysis of crude actin extract before and after precipitation by antiserum (i) by Sephadex G-200 chromatography and (ii) for its stimulating effect on myosin ATPase activity showed that actin was selectively removed.	sephadex	83-97	actin	Oryctolagus cuniculus	187-192