Kinins pp 265-269 | Cite as

Methionyl-Lysyl-Bradykinin: The Kinin Released by Pepsin from Human Kininogens

  • Jorge A. Guimaraes
  • Jack V. Pierce
  • Valdemar Hial
  • John J. Pisano
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)


Since Croxatto and coworkers (1, 2). first described and named the hypotensive, leiomyokinetic peptide released from mammalian serum by pepsin, the identity of pepsitocin has been in question. Habermann and coworkers (3, 4) reported the isolation of two related peptides from pepsin digests of highly purified bovine kininogen: MLBK-Ser-Val-Gln1 (90%) and MLBK-Ser-Val-Gln-Val-Met (10%). In contrast, Hochstrasser and Werle (5) found Gly (or Ser)-Arg-MLBK in pepsin digests of bovine plasma Fraction IV-6. Inasmuch as we had in hand appreciable amounts of highly purified human plasma kininogens (6), we undertook this study of the identity of pepsitocin.


Retention Volume Pepsin Digest Porcine Pepsin Mammalian Serum Peptic Peptide 


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  1. 1.
    Croxatto, H., G. Rojas, and L. Barnafi. Bol. Soc. Biol. Santiago, 8, 84 (1950).Google Scholar
  2. 2.
    Croxatto, H. In Polypeptides which Stimulate Plain Muscle, J.H. Gaddum, ed. Livingstone, Edinburgh & London, p. 92 (1955).Google Scholar
  3. 3.
    Habermann, E. Naunyn-Schmiedebergs Arch. Pharmakol. Exp. Pathol. 253, 474, (1966).Google Scholar
  4. 4.
    Habermann, E. In Hypotensive Peptides, E.G. Erdos, N. Back, and F. Sicuteri, eds. Springer, New York, p. 116 (1966).CrossRefGoogle Scholar
  5. 5.
    Hochstrasser, K. and E. Werle. Hoppe-Seyler’s Z. Physiol. Chem., 348, 177 (1967).CrossRefGoogle Scholar
  6. 6.
    Guimaraes, J.A., R. Chen-Lu, M.E. Webster and J.V. Pierce. Fed. Proc. 33, 641 Abs. (1974).Google Scholar
  7. 7.
    Pierce, J.V. and M. E. Webster. In Hypotensive Peptides, Erdos et al. eds. Springer, New York, p. 130 (1966).CrossRefGoogle Scholar
  8. 8.
    Yano, M., H. Kato, S. Nagasawa and T. Suzuki, J. Biochem. (Tokyo), 62, 386 (1967).Google Scholar
  9. 9.
    Guimaraes, J.A., D. R. Borges, E.S. Prado, and J.L. Prado. Biochem. Pharmacol. 22, 3157 (1973).PubMedCrossRefGoogle Scholar
  10. 10.
    Hial, V., to be published.Google Scholar
  11. 11.
    Sampaio, M.U., M.L. Reis, E. Fink, A.C.M. Camargo, and L. J. Greene. Life Sci. 16, 796 Abs. (1974).CrossRefGoogle Scholar
  12. 12.
    Tamura, Z., T. Nakajima, T. Nakayama, J.J. Pisano, and S. Udenfriend. Anal. Biochem. 52, 595 (1973).PubMedCrossRefGoogle Scholar
  13. 13.
    Elliott, D.F. and G.P. Lewis. Biochem. J. 95, 437 (1965).PubMedGoogle Scholar
  14. 14.
    Guimaraes, J.A., to be published.Google Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Jorge A. Guimaraes
    • 1
  • Jack V. Pierce
    • 1
  • Valdemar Hial
    • 1
  • John J. Pisano
    • 1
  1. 1.Section on Physiological Chemistry, Laboratory of ChemistryNational Heart and Lung Institute, National Institutes of HealthBethesdaUSA

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