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Amino acid sequence from degu islet amyloid-derived insulin shows unique sequence characteristics.

Authors
  • Hellman, U
  • Wernstedt, C
  • Westermark, P
  • O'Brien, T D
  • Rathbun, W B
  • Johnson, K H
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jun 15, 1990
Volume
169
Issue
2
Pages
571–577
Identifiers
PMID: 2192710
Source
Medline
License
Unknown

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 sequence follows: A-chain: GIVDQCCNNICTFNQLQNYCNVP B-chain: YSSQHLCGSNLVEALYMTCGRSGFYRPHD.

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