PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2689170-2	1989	The enzyme procollagen C-proteinase removes the carboxy-terminal propeptide from procollagen.	propeptide	65-75	bone morphogenetic protein 1	Mus musculus	11-35	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	lysyl	4-9	membrane protein, palmitoylated	Mus musculus	107-113	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	lysyl	4-9	replication factor C (activator 1) 5	Mus musculus	224-230	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	lysyl	4-9	solute carrier family 25 (mitochondrial carrier, peroxisomal membrane protein), member 17	Mus musculus	235-241	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	lysyl	4-9	bone morphogenetic protein 1	Mus musculus	242-266	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	10-19	membrane protein, palmitoylated	Mus musculus	107-113	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	10-19	replication factor C (activator 1) 5	Mus musculus	224-230	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	10-19	solute carrier family 25 (mitochondrial carrier, peroxisomal membrane protein), member 17	Mus musculus	235-241	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	10-19	bone morphogenetic protein 1	Mus musculus	242-266	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	155-164	membrane protein, palmitoylated	Mus musculus	107-113	
2689170-6	1989	The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al.	Sepharose	155-164	replication factor C (activator 1) 5	Mus musculus	224-230	
2689170-11	1989	In the course of PP-Sepharose chromatography, a large proportion of the 55-kDa protein disappeared with the concomitant appearance of the smaller enhancer proteins.	Sepharose	20-29	membrane protein, palmitoylated	Mus musculus	72-78