Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca.
Two distinct hypertensive peptides were purified and characterized from Bothrops jararaca (Bj) plasma incubated at pH 4, 37 degrees C, 24 hr. These peptides were active on rat and Bj blood pressure, on rat isolated uterus, on guinea pig isolated ileum and on Bj isolated duodenum. At the releasing conditions no further activities were found for kininases, angiotensinases or angiotensin converting enzymes. The peptides were purified by ethanol/ether extraction, Sephadex G-25 gel filtration, semipreparative reverse-phase (C-18) HPLC and analytical (C-18) HPLC. The amino-acid sequences of the purified peptides corresponded to (Ile5)AII and (Val5-Tyr9)AI and their molecular masses were confirmed by mass spectrometry as 1046.6 and 1348.0 respectively. The presence of those two angiotensins on Bj plasma may have some evolutionary significance since (Ile5)AII is known as a mammalian angiotensin and (Val5)AII as a non-mammalian one.
Borgheresi
R A
RA
Instituto Butantan, Laboratório de Farmacologia, São Paulo, Brazil.
Dalle Lucca
J
J
Carmona
E
E
Picarelli
Z P
ZP
D000595:Amino Acid Sequence; D000804:Angiotensin II; D000818:Animals; D001794:Blood Pressure / Q000187:drug effects; D001798:Blood Proteins / Q000302:isolation & purification* / Q000494:pharmacology*; D017837:Bothrops / Q000097:blood*; D004386:Duodenum; D005260:Female; D006168:Guinea Pigs; D007082:Ileum; D066298:In Vitro Techniques; D008297:Male; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000187:drug effects / Q000502:physiology*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014599:Uterus
D001798:Blood Proteins; D010446:Peptide Fragments; D000804:Angiotensin II