PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9108263-2	1997	Prolyl endopeptidase is one such enzyme, which cleaves on the carboxyl side of proline within peptide substrates.	Proline	79-86	prolyl endopeptidase	Bos taurus	0-20	
7851396-5	1995	This prolyl endopeptidase activity was shown to have a molecular mass (87 kDa) higher than the cytosolic prolyl endopeptidase but, from initial investigation, appears to demonstrate a similarly broad substrate specificity towards proline-containing neuropeptides.	Proline	230-237	prolyl endopeptidase	Bos taurus	5-25	
7851396-5	1995	This prolyl endopeptidase activity was shown to have a molecular mass (87 kDa) higher than the cytosolic prolyl endopeptidase but, from initial investigation, appears to demonstrate a similarly broad substrate specificity towards proline-containing neuropeptides.	Proline	230-237	prolyl endopeptidase	Bos taurus	105-125	
9026355-1	1996	Prolyl endopeptidase has been predominantly described as a cytosolic activity capable of cleaving a number of important neuropeptides (including TRH, LHRH, Bradykinin, Angiotensin, Substance P, Neurotensin, Oxytocin and Vasopressin) on the carboxy side of proline.	Proline	256-263	prolyl endopeptidase	Bos taurus	0-20