Isolation of the tachykinin, Des[Ser1Pro2] scyliorhinin II from the intestine of the ray, Torpedo marmorata

J. Michael Conlon; Lars Thim

doi:10.1016/0016-6480(88)90266-3

Isolation of the tachykinin, Des[Ser¹Pro²] scyliorhinin II from the intestine of the ray, Torpedo marmorata

J. Michael Conlon
, Lars Thim

School of Biomedical Sciences

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

19 Citations (Scopus)

Abstract

A peptide with neurokinin A-like immunoreactivity was isolated from an extract of the intestine of an elasmobranch fish, Torpedo marmorata. The primary structure of the peptide was established as Ser-Asn-Ser-Lys-Cys-Pro-Asp-Gly-Pro-Asp-Cys-Phe-Val-Gly-Leu-Met-NH₂. This amino acid sequence is identical to that of residues (3-18) of scyliorhinin II previously isolated from the intestine of the common dogfish (Scyliorhinus canicula). The presence of the truncated peptide, lacking Ser-Pro, in the Torpedo gut suggests that scyliorhinin II may be a substrate for an enzyme with dipeptidylpeptidase IV-like specificity. The data support previous assertions that strong evolutionary pressure has acted within the elasmobranch subclass of chondrichthyean fish to conserve the structures of regulatory peptides.

Original language	English
Pages (from-to)	383-388
Number of pages	6
Journal	General and Comparative Endocrinology
Volume	71
Issue number	3
DOIs	https://doi.org/10.1016/0016-6480(88)90266-3
Publication status	Published (in print/issue) - Sept 1988

Funding

The work was supported by the Stiftung Volkswa-genwerk. The authors thank Professor N. Hilschmann. Max-Planck-Institut fur Experimentelle Medizin, Gottingen for providing facilities for amino acid analysis; and Professor V. P. Whittaker and Dr. D. V. Agoston, Max-Planck-Institut fur Biophysikalis-the Chemie, Gottingen, for providing the samples of Torpedo gut.

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10.1016/0016-6480(88)90266-3

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title = "Isolation of the tachykinin, Des[Ser1Pro2] scyliorhinin II from the intestine of the ray, Torpedo marmorata",

abstract = "A peptide with neurokinin A-like immunoreactivity was isolated from an extract of the intestine of an elasmobranch fish, Torpedo marmorata. The primary structure of the peptide was established as Ser-Asn-Ser-Lys-Cys-Pro-Asp-Gly-Pro-Asp-Cys-Phe-Val-Gly-Leu-Met-NH2 . This amino acid sequence is identical to that of residues (3-18) of scyliorhinin II previously isolated from the intestine of the common dogfish (Scyliorhinus canicula). The presence of the truncated peptide, lacking Ser-Pro, in the Torpedo gut suggests that scyliorhinin II may be a substrate for an enzyme with dipeptidylpeptidase IV-like specificity. The data support previous assertions that strong evolutionary pressure has acted within the elasmobranch subclass of chondrichthyean fish to conserve the structures of regulatory peptides.",

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AB - A peptide with neurokinin A-like immunoreactivity was isolated from an extract of the intestine of an elasmobranch fish, Torpedo marmorata. The primary structure of the peptide was established as Ser-Asn-Ser-Lys-Cys-Pro-Asp-Gly-Pro-Asp-Cys-Phe-Val-Gly-Leu-Met-NH2 . This amino acid sequence is identical to that of residues (3-18) of scyliorhinin II previously isolated from the intestine of the common dogfish (Scyliorhinus canicula). The presence of the truncated peptide, lacking Ser-Pro, in the Torpedo gut suggests that scyliorhinin II may be a substrate for an enzyme with dipeptidylpeptidase IV-like specificity. The data support previous assertions that strong evolutionary pressure has acted within the elasmobranch subclass of chondrichthyean fish to conserve the structures of regulatory peptides.

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Isolation of the tachykinin, Des[Ser¹Pro²] scyliorhinin II from the intestine of the ray, Torpedo marmorata

Abstract

Funding

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