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Isolation, structure and biological activity of two cholecystokinin octapeptides from sheep brain

Nature volume 274, pages 711713 (17 August 1978) | Download Citation

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Abstract

SEVERAL peptides—for example, substance P and neurotensin—are now known to occur in both endocrine cells of the gut and in central or peripheral neurones1. The significance of this dual distribution is far from fully understood, but it seems possible that the same peptide might function as both hormone and neurotransmitter. Vanderhaeghen et al. have reported that radioimmunoassays (RIA) for the antral hormone gastrin have shown activity in extracts of brain, particularly cerebral cortex, of a wide range of vertebrate species2. However, gastrin has the same COOH-terminal pentapeptide sequence as the intestinal hormone cholecystokinin (CCK) and antisera specific for the COOH terminus of gastrin usually cross-react to some extent with CCK also. We found that the pattern of cross-reactivity of boiling water extracts of brain with six different antisera resembled that of a COOH-terminal fragment of CCK more closely than gastrin, and gel filtration studies have indicated that the main component in the extracts was compatible with the COOH-terminal octapeptide of CCK (CCK8)3; these findings have since been confirmed by others4–6. We have purified from sheep brain two octapeptides corresponding to the CCK-like component previously identified by RIA, and report here the isolation, sequence and some properties of these molecules.

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Author information

Affiliations

  1. Department of Physiology, University of Liverpool, Liverpool, UK

    • G. J. DOCKRAY
    • , R. A. GREGORY
    •  & J. B. HUTCHISON
  2. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK

    • J. IEUAN HARRIS
    •  & M. J. RUNSWICK

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https://doi.org/10.1038/274711a0

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