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Optical Activity and Conformation of Bradykinin and Related Peptides

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Bradykinin and Related Kinins

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 8))

Abstract

The large number of synthetic analogs and homologs of brady-kinin now available have allowed substantial progress in understanding the sequence and specific amino acid residues required for full biological activity. The molecule must contain amino- and carboxylterminal arginines, prolines at positions 2 and 7, and phenylalanine at positions 5 and 81.

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References

  1. J. M. Stewart (1968). Fed. Proc. 27, 63.

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Author information

Authors and Affiliations

  1. Dept. of Medicine, Univ. of Miami School of Medicine, USA

    A. H. Brady & J. W. Ryan

  2. Dept. of Biochemistry, Univ. of Colorado School of Medicine, USA

    J. M. Stewart

Authors
  1. A. H. Brady
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  2. J. M. Stewart
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  3. J. W. Ryan
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Editor information

Editors and Affiliations

  1. Department of Clinical Pharmacology, University of Florence, Florence, Italy

    F. Sicuteri

  2. Department of Pharmacology, Faculty of Medicine of Ribeirao Preto, U.S.P., Sao Paulo, Brazil

    M. Rocha e Silva

  3. Department of Biochemical Pharmacology School of Pharmacy, State University of New York, Buffalo, New York, USA

    Nathan Back

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© 1970 Plenum Press, New York

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Brady, A.H., Stewart, J.M., Ryan, J.W. (1970). Optical Activity and Conformation of Bradykinin and Related Peptides. In: Sicuteri, F., e Silva, M.R., Back, N. (eds) Bradykinin and Related Kinins. Advances in Experimental Medicine and Biology, vol 8. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3198-8_7

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  • DOI: https://doi.org/10.1007/978-1-4684-3198-8_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3200-8

  • Online ISBN: 978-1-4684-3198-8

  • eBook Packages: Springer Book Archive

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