AMINO-ACID-SEQUENCE FROM DEGU ISLET AMYLOID-DERIVED INSULIN SHOWS UNIQUE SEQUENCE CHARACTERISTICS

被引：49

作者：

HELLMAN, U

WERNSTEDT, C

WESTERMARK, P

OBRIEN, TD

RATHBUN, WB

JOHNSON, KH

机构：

[1] LINKOPING UNIV,DEPT PATHOL,S-58183 LINKOPING,SWEDEN

[2] UNIV MINNESOTA,DEPT VET PATHOBIOL,MINNEAPOLIS,MN 55455

[3] UNIV MINNESOTA,DEPT OPHTHALMOL,MINNEAPOLIS,MN 55455

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 169卷 / 02期

关键词：

D O I：

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

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：571 / 577

页数：7

共 20 条

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