Prado E S, Prado de Carvalho L, Araujo-Viel M S, Ling N, Rossier J
Biochem Biophys Res Commun. 1983 Apr 29;112(2):366-71. doi: 10.1016/0006-291x(83)91472-9.
Homogeneous preparations of two well-characterized glandular kallikreins have been examined for their ability to hydrolyze BAM 22P, a methionine-enkephalin-containing-peptide found in the adrenal medulla. Both enzymes cleaved preferentially the Arg6-Arg7 bond in this substrate. The specificity constant (kcat/Km) for this cleavage was 86 mM-1 sec-1 for horse urinary kallikrein and 566 mM-1 sec-1 for porcine pancreatic kallikrein. These results demonstrate a previously undescribed specificity for glandular kallikreins and suggest a possible role for these widely distributed enzymes in prohormone processing.