title: Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases.
abstract: The property of brain endopeptidases of attacking small biologically active polypeptides but not denatured proteins led us to compare them with pancreatic proteolytic enzymes with respect to hydrolysis of a synthetic peptide derived from bradykinin (Gly-Gly-Gly-Arg-bradykinin), free, bound to Affi-Gel 10, or bound to succinylated polylysine of 3,000 and 180,000 daltons, respectively. The data show that brain endopeptidases A and B only hydrolyze bradykinin in its free form, whereas trypsin, chymotrypsin, and carboxypeptidase B hydrolyze the polypeptide both free and covalently bound to a high molecular weight carrier. These results suggest that brain endopeptidases selectively hydrolyze low molecular weight polypeptides.
mesh_terms: D000818:Animals; D001920:Bradykinin; D001921:Brain / Q000201:enzymology*; D002268:Carboxypeptidases / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology*; D011817:Rabbits
chemical_list: D002268:Carboxypeptidases; D010450:Endopeptidases; D002918:Chymotrypsin; D001920:Bradykinin