Characterization of a new inhibitor for angiotensin converting enzyme from the venom of Vipera aspis aspis.
1. Angiotensin converting enzyme inhibitor has been isolated from the venom of Vipera aspis aspis by gel filtration and reverse phase HPLC. 2. The purified inhibitor is a decapeptide, whose amino-terminal is blocked, with mol. wt 1044 determined by fast atom bombardment mass spectrometry. 3. The peptide inhibited the conversion of angiotensin I to angiotensin II, and Ki values were determined to be 7.54 x 10(-4) and 1.36 x 10(-4) M, respectively, using Hip-His-Leu and Hip-Gly-Gly as substrates 4. The peptide also inhibited the degradation of bradykinin, induced hypotension in spontaneously hypertensive rats and caused an increase in capillary permeability in rabbits, however, it possessed no lethality.
Komori
Y
Y
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
Sugihara
H
H
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000008:administration & dosage / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D001794:Blood Pressure / Q000187:drug effects; D007022:Hypotension / Q000188:drug therapy; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D011918:Rats, Inbred SHR; D014757:Viper Venoms / Q000032:analysis*
D000806:Angiotensin-Converting Enzyme Inhibitors; D014757:Viper Venoms; D007703:Peptidyl-Dipeptidase A