PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6215059-2	1982	The protein, SAIP (for serum actin inhibitory protein), has been purified by affinity chromatography of serum over actin-Sepharose followed by protein fractionation with ammonium sulfate and chromatography over DEAE-cellulose.	DEAE-Cellulose	211-225	actin	Oryctolagus cuniculus	29-34	
6233284-3	1984	The purified actin shares many attributes with numerous other actins that have been characterized, including molecular weight, strong binding to DEAE-cellulose, binding to DNase I, reversible polymerization to F-actin, binding of rabbit myosin subfragment 1 to give distinctive arrowheads , formation of Mg paracrystals, and activation of myosin Mg2+-ATPase.	DEAE-Cellulose	145-159	actin	Oryctolagus cuniculus	13-18	
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.	DEAE-Cellulose	33-47	actin	Oryctolagus cuniculus	101-106