| Literature DB >> 6552186 |
E S Prado, L Prado de Carvalho, M S Araujo-Viel, N Ling, J Rossier.
Abstract
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.Entities:
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Year: 1983 PMID: 6552186 DOI: 10.1016/0006-291x(83)91472-9
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575