THE N-TERMINAL SEGMENT OF PROTEIN AA DETERMINES ITS FIBRILLOGENIC PROPERTY

被引：118

作者：

WESTERMARK, GT ^{[1
]}

ENGSTROM, U ^{[1
]}

WESTERMARK, P ^{[1
]}

机构：

[1] LUDWIG INST CANC RES,UPPSALA BRANCH,S-75124 UPPSALA,SWEDEN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 182卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80107-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 amyloid fibril protein AA consists of a varying long N-terminal part of the precursor protein serum AA. By using synthetic peptides corresponding to human and murine protein AA segments and cyanogen bromide fragments of human protein AA, we show evidence that the amyloidogenic part of the molecule is the first 10-15 amino acid long segment. Amino acid substitutions in this part of the molecule may explain why only one of the two mouse SAA isoforms is amyloidogenic. © 1992 Academic Press, Inc.

引用

页码：27 / 33

页数：7

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