CLEAVAGE SPECIFICITIES OF INDIVIDUAL MEMBERS OF KALLIKREIN FAMILY OF PROTEINS ON SYNTHETIC PEPTIDE-CONTAINING THE BRADYKININ SEQUENCE

We have analyzed the effect on bond specificity of various isolated me mbers of the mouse kallikrein family of proteins on a synthetic peptid e containing the bradykinin sequence. The cleavage pattern shows the s elected specificity of these proteases toward the synthetic peptide. T he Phe-His bond (positions 11-12) in the synthetic peptide was favorab ly cleaved by most of the members in this family, including gamma nerv e growth factor. On the other hand, the Lys-Arg bond (position 3-4) wa s found to be susceptible only to gamma-NGF. The combination of these cleavages could result in the degradation of bradykinin in vivo.