Abstract
The main protein of enriched and purified amyloid from Octodon degus pancreatic islets was identified as insulin. The material was reduced and alkylated and the A- and the B-chain were separated by reversed phase chromatography and subjected to Edman degradation and amino acid analysis. It was shown that the A-chain contains two additional C-terminal amino acid residues (i.e. a total of 23 residues) and that the B-chain has a deletion in the C-terminal part (i. e. a total of 29 residues). The obtained sequences follows: • A-chain: GIVDQCCNNICTFNQLQNYCNVP • B-chain: YSSQHLCGSNLVEALYMTCGRSGFYRPHD.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 571-577 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 169 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jun 15 1990 |
Bibliographical note
Funding Information:We thank Dr. David Eaker for performing the amino acid analyses. Supported by the Swedish Medical Research Council (Project No. 5941), the Research Fund of King Gustaf V, the Nordic Insulin Fund, the Louis-Hansen’s Memorial Fund and Grant ROl DK 36734 from the National Institute of Diabetes and Digestive and Kidney Diseases, and Grant ROl EYO503 1 and EYOl197 from the National Eye Institute. We also thank Ingegkd Schiller for preparation of the manuscript.