3.4.15.1 cetyltrimethylammonium bromide 0.1 and 1 mM 732845 3.4.15.1 cetyltrimethylammonium bromide CTAB, activates at 0.1-1.0 mM 755273 3.4.15.1 Cl- - 81241, 81260, 81287 3.4.15.1 Cl- activates 650267, 81212, 81214, 81250, 81264, 81270, 81284 3.4.15.1 Cl- activation, optimal NaCl concentration for the brain enzyme in hydrolysis of LVVYPWTQRY is 10 mM, optimal concentration for hydrolysis of angiotensin I is 200 mM 653416 3.4.15.1 Cl- assay in the presence of zinc and chloride 764572 3.4.15.1 Cl- kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity 667760 3.4.15.1 Cl- nonessential activator over the pH range 5.0-10.0 81233 3.4.15.1 Cl- required 81213, 81247, 81251, 81259 3.4.15.1 Cl- required for hydrolysis of angiotensin I, not required for hydrolysis of bradykinin 81241 3.4.15.1 Diazoacetylnorleucine methyl ester 1.0 mM, activation to 115% of control 650873 3.4.15.1 diisopropylphosphoryl fluoride 1.0 mM, activation to 116.3% of control 650873 3.4.15.1 PCMB slight stimulation 81269 3.4.15.1 SDS 0.1 mM and 10 mM 732845 3.4.15.1 SDS activates at 0.1 mM 755273 3.4.15.1 Soybean trypsin inhibitor 0.5 mM, activation to 115% of control 650873 3.4.15.1 tosylphenylalanine chloromethyl ketone 1.0 mM, activation to 113% of control 650873 3.4.15.1 Triton X-100 0.01% 732845 3.4.15.1 Triton X-100 activates at 0.01%, inhibits at 1.0-10.0% 755273