A novel active pentapeptide from chicken brain identified by antibodies to FMRFamide
| Autor: | Graham J. Dockray, R. J. Gayton, J. Shively, C. S. Barnard, J. R. Reeve |
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| Rok vydání: | 1983 |
| Předmět: |
Brain Chemistry
Antiserum chemistry.chemical_classification Neurotransmitter Agents medicine.medical_specialty Multidisciplinary Tetrapeptide QRFP Neuropeptide Nerve Tissue Proteins Peptide Cross Reactions Biology Pentapeptide repeat Endocrinology chemistry Biochemistry Internal medicine medicine Animals FMRFamide Chickens Oligopeptides Peptide sequence |
| Zdroj: | Nature. 305:328-330 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/305328a0 |
| Popis: | The tetrapeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) and peptides structurally related to it, have been isolated from molluscan ganglia1–3. They have widespread actions on both invertebrate and vertebrate tissues and there is increasing evidence that they are an important group of invertebrate peptide neurotransmitters3–8. It is of interest that the primary amino acid sequence of FMRFamide forms the C-terminal tetrapeptide of an enkephalin-like heptapeptide (Met-enkephalin-Arg6Phe7) isolated from bovine adrenal medulla and striatum9,10. Antisera to FMRFamide have been shown to react in radioimmunoassay and immunohistochemistry with material in the central nervous system of various vertebrate species11–17, but the identity of this material, and in particular its relationship to the opioid heptapeptide, remains uncertain. We have used antibodies specific for the C-terminus of FMRFamide in radioimmunoassays to monitor purification of the material in chicken brain. We describe here the sequence of one of the peptides obtained. It is a biologically active peptide which does not seem to be related to other known vertebrate neuropeptides. |
| Databáze: | OpenAIRE |
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