Abstract
The primary structure of glucagon isolated from the intestine of the common dogfish, Scyliorhinus canicula, was established as 5 10 15 20 25 H S E G T F T S D Y S K Y M D N R R A K D F V Q W L M N T. The peptide shows four substitutions compared with human glucagon: Glu-3 for Gln, Met-14 for Leu, Asn-16 for Ser and Lys-20 for Gln. Glucagon represented the predominant molecular form of the glucagon-like immunoreactivity in the dogfish gut extracts demonstrating that the pathway of posttranslational processing of proglucagon in the gut of this fish differs markedly from the pathway in the mammalian gut.
| Original language | English |
|---|---|
| Pages (from-to) | 50-56 |
| Number of pages | 7 |
| Journal | FEBS Letters |
| Volume | 214 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published (in print/issue) - 6 Apr 1987 |
Funding
This work was supported by the Stiftung Volkswagenwerk. The authorst hank Professor I. Henderson,D epartmento f Zoology, Universityo f Sheffield, for providing dogfish tissuesa nd Professor N. Hilschmann, Max-Planck-Institut fur ExperimentelleM edizin, Gottingen, for providing facilities for amino acid analysis. Antiserum30 K was a gift from Professor R.H. Unger, University of Texas, SouthwesternM edical School, Dallas, Texas, USA, and glicentinw asa gift from Dr A.J. Moody, Novo Research Institute, Bagsvaerd, Denmark.
Keywords
- (Elasmobranch)
- Edman degradation
- HPLC
- Posttranslational processing
- Radioimmunoassay
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