Carassin: A Tachykinin That Is Structurally Related to Neuropeptide-γ from the Brain of the Goldfish |
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Authors: | J Michael Conlon Finbarr O'Harte Richard E Peter Olivier Kah† |
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Institution: | Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178. |
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Abstract: | A 21-amino-acid residue tachykinin-related peptide, carassin, was isolated in pure form from an extract of the brain of the goldfish, Carrassius auratus, by reversed-phase HPLC. The primary structure of the peptide was established as the following: Ser-Pro-Ala-Asn-Ala-Gln-Ile-Thr-Arg-Lys-Arg-His-Lys-Ile-Asn- Ser-Phe-Val-Gly-Leu-Met.NH2. This amino acid sequence is the same length as and shows structural similarity (57% homology) to the mammalian tachykinin, neuropeptide-gamma, which is a product of the posttranslational processing of gamma-preprotachykinin. The mammalian tachykinins, substance P and neurokinin B, were not detected in the extract by using specific antisera directed against the NH2-termini of the peptides, but an antiserum directed against the COOH-terminal region of substance P did detect a low concentration of immunoreactive material. |
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Keywords: | Tachykinin Goldfish brain Neuropeptideγ Scyliorhinin II |
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