PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20335606-4	2010	ATPase activity was evaluated by spectrophotometric measurement of phosphate released from ATP with the use of ammonium molybdate; Na,K-ATPase activity was defined as the portion of total ATPase activity sensitive to ouabain.	Phosphates	67-76	dynein, axonemal, heavy chain 8	Mus musculus	0-6	
19401877-4	2009	ATPase activity of the cells was evaluated by spectrophotometric measurement of phosphate released from ATP with the use of ammonium molybdate, with Na,K-ATPase activity being defined as the portion of total ATPase activity sensitive to ouabain.	Phosphates	80-89	dynein, axonemal, heavy chain 8	Mus musculus	0-6	
19484442-4	2009	ATPase activity of the cells was evaluated by using ammonium molybdate in spectrophotometric measurement of phosphate released from ATP, with Na,K-ATPase activity being defined as the portion of total ATPase activity sensitive to ouabain.	Phosphates	108-117	dynein, axonemal, heavy chain 8	Mus musculus	0-6	
12069596-4	2002	The kinetic constants [concentration of half-maximum activation (inhibition), K(i), and the maximum (minimum) transporter activity, V(i)] were in qualitative and quantitative agreement with those determined earlier for Pgp-ATPase activation monitored by phosphate release in inside-out cellular vesicles and in purified reconstituted systems, respectively.	Phosphates	254-263	dynein, axonemal, heavy chain 8	Mus musculus	223-229	
12069596-7	2002	The micro-pH measurements provide for the first time direct evidence for a tight coupling between the rate of extracellular proton extrusion and intracellular phosphate release upon Pgp-ATPase activation.	Phosphates	159-168	dynein, axonemal, heavy chain 8	Mus musculus	186-192