Isolation and characterization of a new atrial peptide-degrading enzyme from bovine kidney.
An endopeptidase isolated from bovine kidney displays high affinity and selectivity for the Ser-Phe bond located in the C-terminal region of atrial peptides. Enzymatic activity converts APIII and APII to the less active peptide API. This peptidase is inhibited by both metal chelators and sulfhydryl-reactive agents, suggesting both a tightly bound metal and a cysteine residue are important for enzymatic activity. This enzyme may be important for the processing and/or degradation of atrial peptides.
Toll
L
L
Life Sciences Division, SRI International, Menlo Park, CA 94025.
Brandt
S R
SR
Olsen
C M
CM
Judd
A K
AK
Almquist
R G
RG
D000595:Amino Acid Sequence; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism*; D001711:Biotransformation; D002417:Cattle; D002845:Chromatography / Q000379:methods; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D017886:Durapatite; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006882:Hydroxyapatites; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D006882:Hydroxyapatites; D009842:Oligopeptides; D011480:Protease Inhibitors; D009320:Atrial Natriuretic Factor; D017886:Durapatite; D010450:Endopeptidases