Degradation of porcine brain natriuretic peptide (pBNP-26) by endoprotease-24.11 from kidney cortical membranes.
Porcine brain natriuretic peptide of 26 amino acid residues (pBNP-26) is inactivated by endoprotease-24.11 (EC 3.4.24.11) of kidney cortical membranes. In contrast to human alpha atrial natriuretic peptide/cardiodilatin (ANP/CDD) showing a single major cleavage within the disulfide-linked loop between Cys and Phe in position 7 and 8, pBNP-26 is cleaved at several sites. Although both pBNP-26 and ANP/CDD exhibit Cys-Phe peptide bonds at the corresponding positions this bond is not cleaved in BNP-26.
Vogt-Schaden
M
M
Institut für Anatomie und Zellbiologie III, Universität Heidelberg, FRG.
Gagelmann
M
M
Hock
D
D
Herbst
F
F
Forssmann
W G
WG
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004285:Dogs; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D008969:Molecular Sequence Data; D020097:Natriuretic Peptide, Brain; D015260:Neprilysin / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine
D009419:Nerve Tissue Proteins; D020097:Natriuretic Peptide, Brain; D015260:Neprilysin