PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
194900-2	1977	The conditions and utility of the N-chlorosuccinimide/urea (NCS/urea) reagent for the selective cleavage of tryptophanyl peptide bonds in proteins is demonstrated with cytochrome c.	N-chlorosuccinimide	34-53	cytochrome c, somatic	Equus caballus	168-180	
194900-2	1977	The conditions and utility of the N-chlorosuccinimide/urea (NCS/urea) reagent for the selective cleavage of tryptophanyl peptide bonds in proteins is demonstrated with cytochrome c.	N-chlorosuccinimide	60-63	cytochrome c, somatic	Equus caballus	168-180	
194900-3	1977	At low concentrations of NCS/urea the oxidation of thioether side chains in cytochrome c is the predominant reaction.	N-chlorosuccinimide	25-28	cytochrome c, somatic	Equus caballus	76-88	
194900-5	1977	At 10-fold excess of NCS/urea reagent, cleavage of the tryptophanyl peptide bond is optimal at approximately 50% yield in several species of cytochrome c studied.	N-chlorosuccinimide	21-24	cytochrome c, somatic	Equus caballus	141-153