PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18551483-1	1983	Oocystis sp., a unicellular green alga, contained two glutamate dehydrogenase isoenzymes: one was specific for NADH and the other for NADPH.	NADP	134-139	glutamate dehydrogenase 1	Homo sapiens	54-77	
18551483-2	1983	Activity staining after gel electrophoresis indicated that one component in NADH-GDH was not specific for the cofactor and three components in NADPH-GDH.	NADP	143-148	glutamate dehydrogenase 1	Homo sapiens	81-84	
18551483-2	1983	Activity staining after gel electrophoresis indicated that one component in NADH-GDH was not specific for the cofactor and three components in NADPH-GDH.	NADP	143-148	glutamate dehydrogenase 1	Homo sapiens	149-152	
18551483-5	1983	There was a sharp increase in NADPH-GDH activity following the exhaustion of ammonia from the medium but NADH-GDH activity remained unchanged.	NADP	30-35	glutamate dehydrogenase 1	Homo sapiens	36-39	
18551483-6	1983	The NADPH-GDH activity at the outset increased exponentially with time in greenhouse culture but then decreased sharply accompanied by a rapid increase in biomass and nitrite concentration.	NADP	4-9	glutamate dehydrogenase 1	Homo sapiens	10-13	
18551483-7	1983	The K(m) values for ammonia in this algal GDH was high, while glutamate synthase activity was not detected; this suggests that Oocystis may adapt to conditions of ammonia limitation by producing large quantities of NADPH-GDH instead of using glutamate synthase pathway.	NADP	215-220	glutamate dehydrogenase 1	Homo sapiens	42-45	
18551483-7	1983	The K(m) values for ammonia in this algal GDH was high, while glutamate synthase activity was not detected; this suggests that Oocystis may adapt to conditions of ammonia limitation by producing large quantities of NADPH-GDH instead of using glutamate synthase pathway.	NADP	215-220	glutamate dehydrogenase 1	Homo sapiens	221-224