Carassin: A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish

J. Michael Conlon; Finbarr O'Harte; Richard E. Peter; Olivier Kah

doi:10.1111/j.1471-4159.1991.tb11442.x

Carassin: A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish

J. Michael Conlon, Finbarr O'Harte, Richard E. Peter, Olivier Kah

Research output: Contribution to journal › Article › peer-review

40 Citations (Scopus)

Abstract

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 reversedphase HPLC. The primary structure of the peptide was established as the following: Ser‐Pro‐Ala‐Asn‐Ala‐Gln‐IIe‐Thr‐Arg ‐ Lys ‐ Arg ‐ His ‐ Lys ‐ Hle ‐ 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‐γ, which is a product of the posttranslational processing of γ‐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.

Original language	English
Pages (from-to)	1432-1436
Number of pages	5
Journal	Journal of Neurochemistry
Volume	56
Issue number	4
DOIs	https://doi.org/10.1111/j.1471-4159.1991.tb11442.x
Publication status	Published (in print/issue) - Apr 1991

Keywords

Goldfish brain
Neuropeptideγ
Scyliorhinin II
Tachykinin

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10.1111/j.1471-4159.1991.tb11442.x

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title = "Carassin: A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish",

abstract = "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 reversedphase HPLC. The primary structure of the peptide was established as the following: Ser‐Pro‐Ala‐Asn‐Ala‐Gln‐IIe‐Thr‐Arg ‐ Lys ‐ Arg ‐ His ‐ Lys ‐ Hle ‐ 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‐γ, which is a product of the posttranslational processing of γ‐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.",

keywords = "Goldfish brain, Neuropeptideγ, Scyliorhinin II, Tachykinin",

author = "Conlon, {J. Michael} and Finbarr O'Harte and Peter, {Richard E.} and Olivier Kah",

year = "1991",

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doi = "10.1111/j.1471-4159.1991.tb11442.x",

language = "English",

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T2 - A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish

AU - Conlon, J. Michael

AU - O'Harte, Finbarr

AU - Peter, Richard E.

AU - Kah, Olivier

PY - 1991/4

Y1 - 1991/4

N2 - 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 reversedphase HPLC. The primary structure of the peptide was established as the following: Ser‐Pro‐Ala‐Asn‐Ala‐Gln‐IIe‐Thr‐Arg ‐ Lys ‐ Arg ‐ His ‐ Lys ‐ Hle ‐ 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‐γ, which is a product of the posttranslational processing of γ‐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.

AB - 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 reversedphase HPLC. The primary structure of the peptide was established as the following: Ser‐Pro‐Ala‐Asn‐Ala‐Gln‐IIe‐Thr‐Arg ‐ Lys ‐ Arg ‐ His ‐ Lys ‐ Hle ‐ 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‐γ, which is a product of the posttranslational processing of γ‐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.

KW - Goldfish brain

KW - Neuropeptideγ

KW - Scyliorhinin II

KW - Tachykinin

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M3 - Article

C2 - 2002352

AN - SCOPUS:0026090061

SN - 0022-3042

VL - 56

SP - 1432

EP - 1436

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

IS - 4

ER -

Carassin: A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish

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Keywords

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