title: Purification of a membrane-bound metalloendopeptidase from porcine kidney that degrades peptide hormones.
abstract: A porcine kidney microsomal metalloendopeptidase has been enriched 3900-fold. Gel filtration on a calibrated Toyo-Soda G-3000 SW column indicated an appropriate molecular weight for the endopeptidase of 88,000 +/- 2000. The purified enzyme is inhibited by a number of synthetic inhibitors of thermolysin. The endopeptidase hydrolyzes the succinyl (Suc)-containing fluorogenic peptide substrate Suc-Ala-Ala-Phe-(7-amino-4-methylcoumarin) at the Ala-Phe position with a Km of 2.9 X 10(-4) M. The endopeptidase also hydrolyzes a variety of peptides including corticotropin, substance P, angiotensin I and II, neurotensin, somatostatin, bradykinin, and the renin tetradecapeptide substrate. The endopeptidase hydrolyzes both [Leu]- and [Met]enkephalin at the Gly-Phe bond.
mesh_terms: D000818:Animals; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006728:Hormones; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008666:Metalloendopeptidases; D008667:Metalloproteins / Q000302:isolation & purification* / Q000378:metabolism; D008861:Microsomes / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D013552:Swine
chemical_list: D006728:Hormones; D008667:Metalloproteins; D010450:Endopeptidases; D008666:Metalloendopeptidases