Sulphur K-edge XANES spectroscopy of transthyretin amyloid fibres

被引：0
|
作者：
Gales, L
Cardoso, I
Fayard, B
Saraiva, MJ
Damas, AM
机构：
[1] Univ Porto, Inst Ciencias Biomed Abel Salazar, ICBAS, P-4099003 Oporto, Portugal
[2] Univ Porto, Inst Biol Mol & Celular, Grp Estrutura Mol, P-4150 Oporto, Portugal
[3] Univ Porto, Inst Biol Mol & Celular, Grp Amiloide, P-4150 Oporto, Portugal
[4] European Synchrotron Radiat Facil, F-38043 Grenoble, France
来源：
SPECTROSCOPY-AN INTERNATIONAL JOURNAL | 2002年 / 16卷 / 3-4期
关键词：
D O I：
10.1155/2002/589368
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Transthyretin (TTR) amyloidosis results from the self-association of TTR leading to insoluble deposits that occur at the extra cellular level. Sulphur K-edge XANES spectroscopy was used to determine the sulphur oxidation state in transtyretin present in amyloid fibrils. These data is discussed in relation to molecular mechanisms involved in amyloid fibril formation.
引用
收藏
页码：281 / 283
页数：3
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