Characterization of a somatostatin-28 generating metallo-endoprotease from rat brain cytosol

M. C. Beinfeld, J. Bourdais, A. Morel, P. F. Kuks, P. Cohen

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Brain cytosol contains a neutral metallo-protease of about 80,000 which cleaves a substrate containing the site at which mammalian prosomatostatin is cleaved to generate somatostatin 28 in vivo. This represents a cleavage on the carboxyl side of a single arginine residue at an Arg-Ser bond. The enzyme was unable to cleave several other substrates containing single arginine residues or two substrates containing an Arg-Lys or Lys-Arg pair. When it was incubated with anglerfish pancreatic prosomatostatin, it produced significant quantities of a peptide which co-eluted with somatostatin 28 II. Based on the ability of this enzyme to cleave small and large substrates related to somatostatin, it is a potential candidate for the enzymes which cleaves prosomatostatin in vivo
Original languageEnglish
Pages (from-to)968-976
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 1989

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