PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6758860-5	1982	The soluble insulin degrading activity was purified 1400-fold by ammonium sulfate fractionation, molecular exclusion, ion-exchange and affinity chromatography.	Ammonium Sulfate	65-81	insulin	Homo sapiens	12-19	
6663610-6	1983	Insulin binding inhibitors were found in the fraction of the serum precipitated by ammonium sulphate.	Ammonium Sulfate	83-100	insulin	Homo sapiens	0-7	
6271619-5	1981	The serum inhibitors of both insulin and SM-C binding were precipitated equally by Staph-A and also by 40% ammonium sulfate, suggesting they were immunoglobulins.	Ammonium Sulfate	107-123	insulin	Homo sapiens	29-36	
6123319-5	1982	The persistence of the effect of insulin through high dilution of tissue extracts and through purification involving precipitation with (NH4)2SO4 suggests that the enzyme undergoes a covalent modification after exposure of intact tissue to the hormone.	Ammonium Sulfate	136-145	insulin	Homo sapiens	33-40	
4504339-2	1972	The presumed insulin recepotr, which is extracted from these membranes in soluble form with Triton X-100, can be further purified by ammonium sulfate fractionation (3-fold purification) or by diethylaminoethyl-cellulose chromatography (60-fold purification).	Ammonium Sulfate	133-149	insulin	Homo sapiens	13-20