Amino acid sequence from degu islet amyloid-derived insulin shows unique sequence characteristics.
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.
Ludwig Institute for Cancer Research, Uppsala Branch, Sweden.
U
U
Hellman
C
C
Wernstedt
P
P
Westermark
T D
TD
O'Brien
W B
WB
Rathbun
K H
KH
Johnson
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007328:Insulin / Q000235:genetics* / Q000302:isolation & purification; D007515:Islets of Langerhans / Q000032:analysis; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D012377:Rodentia / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D007328:Insulin; D046911:Macromolecular Substances