Inhibition of aspartic proteinases by synthetic peptides derived from the propart region of human prorenin.
1. Five synthetic peptides which together spanned the propart segment of human prorenin were tested for their ability to interact with human renin, pepsin, gastricsin, cathepsin D, cathepsin E, calf chymosin and the aspartic proteinase from Endothia parasitica. 2. While two peptides showed no significant effect with any of the enzymes, a further two were cleaved by several enzymes. 3. Only one (corresponding to the 32P-43P residues in the propart sequence) acted as a weak competitive inhibitor of most of the enzymes.
Richards
A D
AD
Department of Biochemistry, University of Wales College of Cardiff.
Kay
J
J
Dunn
B M
BM
Bessant
C M
CM
Charlton
P A
PA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors*; D002417:Cattle; D004792:Enzyme Precursors / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D012083:Renin / Q000737:chemistry / Q000502:physiology*
D000596:Amino Acids; D004792:Enzyme Precursors; D010455:Peptides; D016282:Aspartic Acid Endopeptidases; D012083:Renin