PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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