Abstract
Pancreatic tissue of the channel catfish (Ictalurus punctatus) contains two somatostatins. The amino acid sequence of a 14-residue containing peptide (SS-14) is identical in sequence and has the same mass ion by fast atom bombardment mass spectrometry as mammalian SS-14. A 22-residue somatostatin (SS-22) has also been isolated and its amino acid sequence determined. The amino acid sequence differs from that reported by Oyama et al. (J Biol Chem 255:2251, 1980) in two of the 22-residues (positions 5 and 19). Somatostatin-22 is a glycoprotein, with carbohydrate attached at Thr-5. Several 22-residue peptides have been purified and all of them have identical amino acid compositions and different carbohydrate structure and/or composition. SS-22 has 7 amino acid residues which are identical to those observed in SS-14. The nucleotide sequence of the two cDNAs coding for SS-14 and SS-22 have been determined. The mRNAs encode precursors to SS-14 and SS-22 of 114 and 105 residues, respectively. The two precursors also have different amino acid sequence at the site of prohormone proteolytic processing. Analysis of genomic DNA reveals that SS-14 and SS-22 sequences are present on different restriction fragments and thus are encoded by separate genes.
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References
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© 1985 Springer Science+Business Media New York
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Dixon, J.E., Andrews, P.C. (1985). Somatostatins of the Channel Catfish. In: Patel, Y.C., Tannenbaum, G.S. (eds) Somatostatin. Advances in Experimental Medicine and Biology, vol 188. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7886-4_2
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DOI: https://doi.org/10.1007/978-1-4615-7886-4_2
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