PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8193137-3	1994	In the present study, we investigated the role of N- and O-glycosylation in intracellular transport and extracellular cleavage-secretion of rabbit testicular ACE.	Nitrogen	50-51	angiotensin-converting enzyme	Oryctolagus cuniculus	158-161	
8193137-7	1994	Our experiments demonstrated that newly synthesized ACE acquires both N- and O-linked sugars before its cleavage-secretion and complete blockage of glycosylation results in rapid intracellular turnover of underglycosylated ACE.	n- and o-linked sugars	70-92	angiotensin-converting enzyme	Oryctolagus cuniculus	52-55	
8193137-8	1994	However, ACE synthesized without N-linked complex sugars and O-linked sugars can undergo normal transport and cleavage-secretion, and the underglycosylated protein is enzymatically active.	Nitrogen	33-34	angiotensin-converting enzyme	Oryctolagus cuniculus	9-12	
8193137-8	1994	However, ACE synthesized without N-linked complex sugars and O-linked sugars can undergo normal transport and cleavage-secretion, and the underglycosylated protein is enzymatically active.	Sugars	50-56	angiotensin-converting enzyme	Oryctolagus cuniculus	9-12	
8193137-8	1994	However, ACE synthesized without N-linked complex sugars and O-linked sugars can undergo normal transport and cleavage-secretion, and the underglycosylated protein is enzymatically active.	o-linked sugars	61-76	angiotensin-converting enzyme	Oryctolagus cuniculus	9-12