Abstract
THE venom from Bothrops jararaca contains enzymes which liberate kinins from plasma kininogen1. Ferreira2 found that the venom also contained a peptidic fraction (bradykinin potentiating factor, BPF) which potentiated the actions of bradykinin on various isolated organs and on the blood pressure of the cat. This potentiating action was later correlated with an inhibition of kinin-destroying enzymes3–5. Recently BPF has been separated into several different active fractions and the amino-acid composition of nine purified peptides has been established6. The structure of the smallest of the peptides (V-3A), a pentapeptide, has been established (pGa-Lys-Trp-Ala-Pro) and the material has been synthesized7. Ferreira, Bartelt and Greene6 also measured the bradykinin-potentiating activity of these different purified peptides on the isolated ileum from the guinea-pig as an indication of their ability to inhibit kininases.
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References
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The erratum article can be found online at https://doi.org/10.1038/225981c0
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FERREIRA, S., GREENE, L., ALABASTER, V. et al. Activity of Various Fractions of Bradykinin Potentiating Factor against Angiotensin I Converting Enzyme. Nature 225, 379–380 (1970). https://doi.org/10.1038/225379a0
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DOI: https://doi.org/10.1038/225379a0
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