PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9711466-3	1998	(a) The substrate of phospholipase A2 1-octadecanoyl 2-[14C]eicosatetraenoyl-sn-glycero-3-phosphocholine ([14C]20:4-GPC) was added to the culture medium.	Carbon-14	56-59	phospholipase A2 group IB	Rattus norvegicus	21-37	
11551515-6	2001	The phospholipase A(2) (PLA(2)) inhibitor, mepacrine, completely inhibited the [14C]-AA response.	Carbon-14	80-83	phospholipase A2 group IB	Rattus norvegicus	4-22	
11551515-6	2001	The phospholipase A(2) (PLA(2)) inhibitor, mepacrine, completely inhibited the [14C]-AA response.	Carbon-14	80-83	phospholipase A2 group IB	Rattus norvegicus	24-30	
11551515-11	2001	We conclude that TBHP stimulates the release of [14C]-AA from membrane phospholipids through a PLA(2)-mediated mechanism.	Carbon-14	49-52	phospholipase A2 group IB	Rattus norvegicus	95-101	
9711466-5	1998	(b) Extracellular fluids were separated from the macrophages and incubated with [14C]20:4-GPC: 48% of the dose was hydrolyzed by extracellular fluid-associated secreted phospholipase A2 and decyloctyl-GPC at 3 microM, reduced this hydrolysis by 50%.	Carbon-14	81-84	phospholipase A2 group IB	Rattus norvegicus	169-185	
9171179-12	1997	The tissue was homogenized and the PLA2 activity was determined using [14C]arachidonate-labeled Escherichia coli phospholipid membrane as a substrate.	Carbon-14	71-74	phospholipase A2 group IB	Rattus norvegicus	35-39	
8436962-5	1993	GCP phospholipase A2 (PLA2) activity was demonstrated using [3H]-or [14C]AA-phosphatidylcholine (PC) or -PI as the substrate in vitro and GCPs or a cytosolic GCP extract as the source of enzyme.	Carbon-14	69-72	phospholipase A2 group IB	Rattus norvegicus	4-20	
8662651-5	1996	Under conditions where the OMV stay intact, externally added phospholipase A2 is able to hydrolyze up to 50% of both the introduced [14C]PC and the endogenous PC.	Carbon-14	133-136	phospholipase A2 group IB	Rattus norvegicus	61-77	
8725048-3	1995	The activity of phospholipase A2 (PLA2) was determined by monitoring 14C] arachidonate release using 14C] phosphatidylcholine (PC) or 14C] phosphatidylethanolamine (PE) as a substrate.	Carbon-14	69-72	phospholipase A2 group IB	Rattus norvegicus	16-32	
8725048-3	1995	The activity of phospholipase A2 (PLA2) was determined by monitoring 14C] arachidonate release using 14C] phosphatidylcholine (PC) or 14C] phosphatidylethanolamine (PE) as a substrate.	Carbon-14	69-72	phospholipase A2 group IB	Rattus norvegicus	34-38	
8436962-5	1993	GCP phospholipase A2 (PLA2) activity was demonstrated using [3H]-or [14C]AA-phosphatidylcholine (PC) or -PI as the substrate in vitro and GCPs or a cytosolic GCP extract as the source of enzyme.	Carbon-14	69-72	phospholipase A2 group IB	Rattus norvegicus	22-26	
6810947-8	1982	Deoxycholate also induces slightly the disappearance of some 14C radioactivity from phosphatidylethanolamine and phosphatidylcholine, which might reflect activation of phospholipase A2.	Carbon-14	61-64	phospholipase A2 group IB	Rattus norvegicus	168-184	
3040878-4	1987	The 3H/14C ratio decreased in PI in a time-dependent manner, suggesting the involvement of a phospholipase A2 activity.	Carbon-14	7-10	phospholipase A2 group IB	Rattus norvegicus	93-109	
3094537-2	1986	Phospholipase A2 activity of these preparations was determined by measuring either the release of [3H]arachidonic acid from cellular phospholipids prelabeled with [3H]arachidonic acid or by measuring the formation of [14C]lysophosphatidylethanolamine from cellular lipids prelabeled with [14C]ethanolamine.	Carbon-14	217-222	phospholipase A2 group IB	Rattus norvegicus	0-16	
6139416-2	1983	The phospholipase A2 stimulation, dependent on calcium, was elicited in resting synaptosomes by A23187 and was demonstrated with incorporated 1-acyl-2-[14C]oleoyl-phosphatidylcholine but not with incorporated [14C]phosphatidylethanolamine or [14C]phosphatidylserine.	Carbon-14	152-155	phospholipase A2 group IB	Rattus norvegicus	4-20