PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2759096-3	1989	At this temperature, aminopeptidase N (EC 3.4.11.2) and sucrase-isomaltase (EC 3.2.1.48-10) both accumulated intracellularly, predominantly in their transient, high mannose-glycosylated form characteristic of the newly synthesized enzymes prior to the molecular processing taking place in the Golgi complex.	Mannose	165-172	sucrase-isomaltase	Sus scrofa	56-74	
2864287-3	1985	The conversion from transient (high mannose glycosylated) to mature (complex glycosylated) form was 1.7-times slower for sucrase-isomaltase than for aminopeptidase N, indicating a slower rate of migration from the rough endoplasmic reticulum to the Golgi complex.	Mannose	36-43	sucrase-isomaltase	Sus scrofa	121-139	
6363129-5	1984	Treatment of aminopeptidase N and sucrase-isomaltase with endo F reduced the size of the high mannose forms approximately to those seen in the presence of tunicamycin.	Mannose	94-101	sucrase-isomaltase	Sus scrofa	34-52