Letter | Published:

A monomeric insulin from the porcupine (Hystrix cristata), an Old World hystricomorph

Nature volume 286, pages 822824 (21 August 1980) | Download Citation

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Abstract

The insulins of New World hystricomorph rodents exhibit many novel amino acid changes in primary structure when compared with other mammalian insulins1–3. These changes give rise to unusual properties (low potency, failure to self-associate4–6) not shared by other naturally-occurring insulins. We report here on the primary structure, zinc-binding properties and circular dichroism (CD) of porcupine insulin (Hystrix cristata), the first Old World hystricomorph insulin to be investigated, and discuss the changes in primary structure of the hormone in relation to its properties. Residue B22 is strongly implicated as being responsible for the unusual properties of porcupine insulin.

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Affiliations

  1. Laboratory of Molecular Biology, Department of Crystallography, The Wellcome Foundation Ltd, Temple Hill, Dartford, Kent DA1 5AH, UK

    • R. Horuk
    •  & T. L. Blundell
  2. Biochemical Research Department, The Wellcome Foundation Ltd, Temple Hill, Dartford, Kent DA1 5AH, UK

    • N. R. Lazarus
    •  & R. W. J. Neville
  3. Protein Chemistry R&D, Wellcome Research Laboratories, Langley Court, Beckenham, Kent, UK

    • D. Stone
  4. Fachgebiet Struktur und Funktion der Proteine, Abteilung Physiologische Chemie, Rheinisch-Westfälische Technische Hochschule, D-5100 Aachen, FRG

    • A. Wollmer

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https://doi.org/10.1038/286822a0

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