Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca

Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca

Autor Borgheresi, RAMB Google Scholar
DalleLucca, J. Google Scholar
Carmona, E. Google Scholar
Picarelli, Z. P. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo 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 (Ile(5))AII and (Val(5)-Tyr(9))AI and their molecular masses were confirmed by mass spectrometry as 1046.6 and 1348.0 respectively. the presence oi those two angiotensins on Bj plasma may have some evolutionary significance since (Ile(5))AII is known as a mammalian angiotensin and (Val(5))AII as a non-mammalian one.
Palavra-chave amino-acid sequences
angiotensins
Bothrops jararaca snake
identification
peptide formation
renin angiotensin system
plasma
vasoactive peptides
Idioma Inglês
Data de publicação 1996-03-01
Publicado em Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. Oxford: Pergamon-Elsevier B.V., v. 113, n. 3, p. 467-473, 1996.
ISSN 0305-0491 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 467-473
Fonte http://dx.doi.org/10.1016/0305-0491(95)02072-1
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1996UC56400005
Endereço permanente http://repositorio.unifesp.br/handle/11600/25562

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