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

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.

authors

Hellman U,Wernstedt C,Westermark P,O'Brien TD,Rathbun WB,Johnson KH

doi

10.1016/0006-291x(90)90369-x

subject

Has Abstract

pub_date

1990-06-15 00:00:00

pages

571-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)90369-X

journal_volume

169

pub_type

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