PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3601232-2	1987	MAO-A was found to be markedly inhibited by BQ competitively with the substrate, kynuramine, while MAO-B was less sensitive to this inhibitor and the inhibition was non-competitive with the substrate.	quinone	44-46	monoamine oxidase A	Rattus norvegicus	0-5	
3601232-3	1987	The Ki value of MAO-A (9.62 +/- 0.35 microM) was much smaller than the Km value of the enzyme with the substrate (56.3 +/- 3.5 microM) or the Ki value of MAO-B with BQ (20.3 +/- 0.9 microM).	quinone	165-167	monoamine oxidase A	Rattus norvegicus	16-21	
3601232-4	1987	The inhibition of MAO-A by BQ was also confirmed by the use of platelet mitochondria and clonal rat pheochromocytoma PC12h cells as enzyme sources.	quinone	27-29	monoamine oxidase A	Rattus norvegicus	18-23	
3601232-5	1987	The inhibition of MAO activity by BQ proved to be reversible: the inhibited enzyme activity could be recovered by column chromatography on Sephadex G-25.	quinone	34-36	monoamine oxidase A	Rattus norvegicus	18-21