PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11563960-3	2001	The interaction of the enzyme with the inhibitor strongly depended on the presence of chloride in the medium, and the apparent dissociation constant of the ACE-chloride complex was (1.3 +/- 0.2).10(-3) M for the somatic enzyme.	Chlorides	86-94	angiotensin I converting enzyme	Bos taurus	156-159	
8300752-5	1993	Increasing chloride concentration in the assay buffer resulted in an increase in BBECs ACE activity of 63%.	Chlorides	11-19	angiotensin I converting enzyme	Bos taurus	81-90	
16271036-0	2005	Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme.	Chlorides	12-20	angiotensin I converting enzyme	Bos taurus	64-93	
16271036-1	2005	Modeling the structure of the C-domain of bovine angiotensin-converting enzyme revealed two putative chloride-binding sites.	Chlorides	101-109	angiotensin I converting enzyme	Bos taurus	49-78	
16271036-4	2005	A general scheme for the effect of chloride anions on activity of the C-domain of bovine angiotensin-converting enzyme accounting for binding the "activating" and "inhibiting" anions is suggested.	Chlorides	35-43	angiotensin I converting enzyme	Bos taurus	89-118	
10887282-4	2000	The influence of chloride and sulfate anions on the enzymatic activity of this fragment has been investigated, and kinetic parameters for hydrolysis of synthetic tripeptide substrates catalyzed by the N-domain of ACE have been determined.	Chlorides	17-25	angiotensin I converting enzyme	Bos taurus	213-216