Rabbit brain thiol-activated endopeptidase. Hydrolysis of bradykinin and kininogen

A neutral brain endopeptidase which hydrolyzes bradykinin (Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) at the Phe5-Ser6 peptide bond was activated about 10 times by dithiothreitol. The preferential specificity of the enzyme for small peptides was suggested on the basis of the absence of activity toward a bradykinin-related protein such as S-carboxymethylated plasma kininogen.