PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22835833-3	2012	For method validation, dithiothreitol-reduced bovine insulin as a model molecule was incubated with either BITC or PEITC, and digested peptides were analyzed by ultra-performance liquid chromatography time-of-flight mass spectrometry (UPLC-TOF-MS) and liquid chromatography quadrupole TOF-MS (LC-Q-TOF-MS).	Dithiothreitol	23-37	insulin	Bos taurus	53-60	
3793398-8	1986	In contrast, when the cross-linked 125I-insulin-protein complexes were first reduced with dithiothreitol (DTT) and then subjected to SDS-PAGE, the 560,000-Da complex from retinal microvessels was dissociated into a 125,000-Da subunit, which is identical in size to the alpha-subunit of the insulin receptor reported in other tissues, while the 560,000-Da complex from nonvascular retinal tissue was dissociated into a 116,000-Da subunit.	Dithiothreitol	90-104	insulin	Bos taurus	40-47	
3793398-8	1986	In contrast, when the cross-linked 125I-insulin-protein complexes were first reduced with dithiothreitol (DTT) and then subjected to SDS-PAGE, the 560,000-Da complex from retinal microvessels was dissociated into a 125,000-Da subunit, which is identical in size to the alpha-subunit of the insulin receptor reported in other tissues, while the 560,000-Da complex from nonvascular retinal tissue was dissociated into a 116,000-Da subunit.	Dithiothreitol	106-109	insulin	Bos taurus	40-47	
3793398-8	1986	In contrast, when the cross-linked 125I-insulin-protein complexes were first reduced with dithiothreitol (DTT) and then subjected to SDS-PAGE, the 560,000-Da complex from retinal microvessels was dissociated into a 125,000-Da subunit, which is identical in size to the alpha-subunit of the insulin receptor reported in other tissues, while the 560,000-Da complex from nonvascular retinal tissue was dissociated into a 116,000-Da subunit.	Dithiothreitol	106-109	insulin	Bos taurus	290-297	
2868714-3	1986	The properties of the technique are illustrated by an investigation of cleavage reactions of the disulfide bonds in bovine insulin, cyclic somatostatin, and conotoxin G1 utilizing the reducing agent dithiothreitol.	Dithiothreitol	199-213	insulin	Bos taurus	123-169	
11735414-7	2001	H3 activates more than 60-fold degradation of the oxidized B-chain of insulin, by cleaving mainly bonds after acidic and branched chain amino acids, and accelerates the degradation of casein and lysozyme, the latter in the presence of dithiothreitol.	Dithiothreitol	235-249	insulin	Bos taurus	70-77	
15739495-3	1997	The denaturation of bovine insulin was carried in dithiothreitol solution at 100 degrees C, and the equilibrium products were examined by HPLC at different reaction time.	Dithiothreitol	50-64	insulin	Bos taurus	27-34	
9314099-3	1997	Upon incubation with dithiothreitol, di- and tri-fluoresceinthiocarbamyl-insulin evinced the highest and the lowest enhancement of fluorescence emission, whereas the mono-substituted protein had intermediate enhancement.	Dithiothreitol	21-35	insulin	Bos taurus	73-80