PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8485108-0	1993	Refined structure of the aminobenzolamide complex of human carbonic anhydrase II at 1.9 A and sulphonamide modelling of bovine carbonic anhydrase III.	Sulfonamides	94-106	carbonic anhydrase 3	Bos taurus	127-149
8485108-9	1993	In modelling studies of bovine carbonic anhydrase III (BCA III) it was evident that Phe 198 prevents an optimal interaction with sulphonamides.	Phenylalanine	84-87	carbonic anhydrase 3	Bos taurus	31-53
8485108-9	1993	In modelling studies of bovine carbonic anhydrase III (BCA III) it was evident that Phe 198 prevents an optimal interaction with sulphonamides.	Sulfonamides	129-142	carbonic anhydrase 3	Bos taurus	31-53
3097002-1	1986	Crystals of bovine carbonic anhydrase III have been grown in a solution of polyethylene glycol.	Polyethylene Glycols	75-94	carbonic anhydrase 3	Bos taurus	19-41
3128444-1	1988	The binding of N3- to Co(II)-substituted bovine carbonic anhydrase III was measured at various pH values by spectrophotometric titrations.	Cobalt(2+)	22-28	carbonic anhydrase 3	Bos taurus	48-70
3128444-9	1988	Our results strongly support the hypothesis that the rate-limiting step in CO2 hydration catalyzed by carbonic anhydrase III is the protolysis of metal-bound water.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	75-78	carbonic anhydrase 3	Bos taurus	102-124
3128444-9	1988	Our results strongly support the hypothesis that the rate-limiting step in CO2 hydration catalyzed by carbonic anhydrase III is the protolysis of metal-bound water.	Metals	146-151	carbonic anhydrase 3	Bos taurus	102-124
3128444-9	1988	Our results strongly support the hypothesis that the rate-limiting step in CO2 hydration catalyzed by carbonic anhydrase III is the protolysis of metal-bound water.	Water	158-163	carbonic anhydrase 3	Bos taurus	102-124
3103674-0	1986	Molecular basis of the oxygen exchange from CO2 catalyzed by carbonic anhydrase III from bovine skeletal muscle.	Oxygen	23-29	carbonic anhydrase 3	Bos taurus	61-83
3103674-0	1986	Molecular basis of the oxygen exchange from CO2 catalyzed by carbonic anhydrase III from bovine skeletal muscle.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	44-47	carbonic anhydrase 3	Bos taurus	61-83
3103674-3	1986	Using membrane-inlet mass spectrometry, we have measured 18O exchange between CO2 and H2O catalyzed by native zinc-containing and cobalt(II)-substituted carbonic anhydrase III from bovine skeletal muscle near pH 7.5.	18o	57-60	carbonic anhydrase 3	Bos taurus	153-175
3103674-3	1986	Using membrane-inlet mass spectrometry, we have measured 18O exchange between CO2 and H2O catalyzed by native zinc-containing and cobalt(II)-substituted carbonic anhydrase III from bovine skeletal muscle near pH 7.5.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	78-81	carbonic anhydrase 3	Bos taurus	153-175
3103674-3	1986	Using membrane-inlet mass spectrometry, we have measured 18O exchange between CO2 and H2O catalyzed by native zinc-containing and cobalt(II)-substituted carbonic anhydrase III from bovine skeletal muscle near pH 7.5.	Water	86-89	carbonic anhydrase 3	Bos taurus	153-175
3103674-3	1986	Using membrane-inlet mass spectrometry, we have measured 18O exchange between CO2 and H2O catalyzed by native zinc-containing and cobalt(II)-substituted carbonic anhydrase III from bovine skeletal muscle near pH 7.5.	Cobalt(2+)	130-140	carbonic anhydrase 3	Bos taurus	153-175
1898739-1	1991	We have found that many dianionic species, at millimolar concentrations, significantly activate or inhibit the bovine carbonic anhydrase III-catalyzed hydration of CO2.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	164-167	carbonic anhydrase 3	Bos taurus	118-140
1898739-4	1991	Our kinetic data are consistent with a formal mechanism of action for carbonic anhydrase III that is directly analogous to that of carbonic anhydrase II, in which Lys-64 of carbonic anhydrase III can act as an intramolecular H+ transfer group during CO2 hydration.	Lysine	163-166	carbonic anhydrase 3	Bos taurus	70-92
1898739-4	1991	Our kinetic data are consistent with a formal mechanism of action for carbonic anhydrase III that is directly analogous to that of carbonic anhydrase II, in which Lys-64 of carbonic anhydrase III can act as an intramolecular H+ transfer group during CO2 hydration.	Lysine	163-166	carbonic anhydrase 3	Bos taurus	173-195
1898739-4	1991	Our kinetic data are consistent with a formal mechanism of action for carbonic anhydrase III that is directly analogous to that of carbonic anhydrase II, in which Lys-64 of carbonic anhydrase III can act as an intramolecular H+ transfer group during CO2 hydration.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	250-253	carbonic anhydrase 3	Bos taurus	70-92
1898739-4	1991	Our kinetic data are consistent with a formal mechanism of action for carbonic anhydrase III that is directly analogous to that of carbonic anhydrase II, in which Lys-64 of carbonic anhydrase III can act as an intramolecular H+ transfer group during CO2 hydration.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	250-253	carbonic anhydrase 3	Bos taurus	173-195
3090030-0	1986	Hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle.	4-nitrophenyl acetate	14-35	carbonic anhydrase 3	Bos taurus	49-71
3090030-1	1986	We report three experiments which show that the hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle occurs at a site on the enzyme different than the active site for CO2 hydration.	4-nitrophenyl acetate	62-83	carbonic anhydrase 3	Bos taurus	97-119
3090030-1	1986	We report three experiments which show that the hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle occurs at a site on the enzyme different than the active site for CO2 hydration.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	214-217	carbonic anhydrase 3	Bos taurus	97-119
3090030-4	1986	The apoenzyme of carbonic anhydrase III, which is inactive in the catalytic hydration of CO2, was found to be as active in the hydrolysis of 4-nitrophenyl acetate as native isozyme III.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	89-92	carbonic anhydrase 3	Bos taurus	17-39
3090030-4	1986	The apoenzyme of carbonic anhydrase III, which is inactive in the catalytic hydration of CO2, was found to be as active in the hydrolysis of 4-nitrophenyl acetate as native isozyme III.	4-nitrophenyl acetate	141-162	carbonic anhydrase 3	Bos taurus	17-39
6428265-4	1984	The dissociation constants were measured for 7-acetamido-2-(4"-sulfamylphenylazo)-1-hydroxynaphthalene-3, 6-disulfonate (Neoprontosil) complexes with carbonic anhydrase isozymes CA I, CA II, and CA III from bovine and human sources, and chicken CA III from skeletal muscle.	7-acetamido-2-(4"-sulfamylphenylazo)-1-hydroxynaphthalene-3, 6-disulfonate	45-119	carbonic anhydrase 3	Bos taurus	195-201
3929690-6	1985	Bovine carbonic anhydrase III contains five thiol groups, two of which react readily with Ellman"s reagent without effect on the catalytic activity.	Sulfhydryl Compounds	44-49	carbonic anhydrase 3	Bos taurus	7-29