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.
|Number of pages||5|
|Journal||Journal of Neurochemistry|
|Publication status||Published (in print/issue) - Apr 1991|
- Goldfish brain
- Scyliorhinin II