PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8843796-5	1996	Activities of angiotensin-converting enzyme (ACE) and 5"-nucleotidase (NCT) were assayed in Earle"s balanced salts solution utilizing [3H]benzoyl-Phe-Ala-Pro ([3H]BPAP) and 5"-[14C]AMP as substrates, respectively.	bpap	163-167	angiotensin I converting enzyme	Bos taurus	14-43	
8843796-6	1996	Under first-order reaction conditions and at constant substrate concentrations ([BPAP] = 15 nM, [AMP] = 1 microM), Vmax/K(m) ratios of ACE and NCT declined to 20% of their original values, as Vm increased from 0.6 to 2 ml.	bpap	81-85	angiotensin I converting enzyme	Bos taurus	135-138	
8843796-7	1996	ACE activity was also studied at constant substrate mass (BPAP = 7 pmol) under first-order reaction conditions.	bpap	58-62	angiotensin I converting enzyme	Bos taurus	0-3	
8843796-9	1996	Under zero-order reaction conditions ([BPAP] = 250 microM), ACE activity (Vmax) was similarly related to Vm.	bpap	39-43	angiotensin I converting enzyme	Bos taurus	60-63	
2159223-6	1990	The apparent kinetics of BPAP metabolism were determined by four models used previously to determine pulmonary endothelial ACE kinetics in vivo, the most useful model incorporating transit time heterogeneity.	bpap	25-29	angiotensin I converting enzyme	Bos taurus	123-126