PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2849453-5	1988	Binding of 3H-ramiprilat was also inhibited by increasing concentrations of enalaprilat, another ACE-inhibitor or by preincubation of the glomeruli with polyclonal antibodies against ACE.	3h-ramiprilat	11-24	angiotensin I converting enzyme	Homo sapiens	97-100	
9788827-2	1998	METHODS AND RESULTS: Radioligand binding with 3H-ramiprilat was used to measure ACE protein in membrane preparations of hearts obtained from 36 subjects with idiopathic dilated cardiomyopathy (IDC), 8 subjects with primary pulmonary hypertension (PPH), and 32 organ donors with normal cardiac function (NF hearts).	3h-ramiprilat	46-59	angiotensin I converting enzyme	Homo sapiens	80-83	
2849453-5	1988	Binding of 3H-ramiprilat was also inhibited by increasing concentrations of enalaprilat, another ACE-inhibitor or by preincubation of the glomeruli with polyclonal antibodies against ACE.	3h-ramiprilat	11-24	angiotensin I converting enzyme	Homo sapiens	183-186	
2849453-10	1988	In conclusion, the binding of 3H-ramiprilat to isolated human glomeruli is specific and resembles the characteristics which have been found earlier for enzyme activity of ACE.	3h-ramiprilat	30-43	angiotensin I converting enzyme	Homo sapiens	171-174	
2849453-11	1988	Thus, binding of 3H-ramiprilat to isolated glomeruli can be assumed to be directed to ACE.	3h-ramiprilat	17-30	angiotensin I converting enzyme	Homo sapiens	86-89