PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16667568-4	1990	The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively.	Phenylglyoxal	63-66	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	164-169	
16667568-4	1990	The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively.	Phenylglyoxal	126-129	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	164-169	
16667568-7	1990	The double logarithm plots of pseudo-first order rate constant versus reagent concentrations gave slopes of 0.88 (PGO) and 0.90 (BD), respectively, suggesting that the inactivation may possibly result from reaction of at least one arginyl residue at the active site of H(+)-translocating PPase.	Phenylglyoxal	114-117	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	288-293