TY - JOUR
T1 - Isolation of the tachykinin, Des[Ser1Pro2] scyliorhinin II from the intestine of the ray, Torpedo marmorata
AU - Conlon, J. Michael
AU - Thim, Lars
N1 - Funding Information:
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.
PY - 1988/9
Y1 - 1988/9
N2 - 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.
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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U2 - 10.1016/0016-6480(88)90266-3
DO - 10.1016/0016-6480(88)90266-3
M3 - Article
C2 - 2847952
AN - SCOPUS:0023719635
SN - 0016-6480
VL - 71
SP - 383
EP - 388
JO - General and Comparative Endocrinology
JF - General and Comparative Endocrinology
IS - 3
ER -