論文

査読有り
2010年

SAXS and SANS Observations of Abnormal Aggregation of Human alpha-Crystallin

CHEMISTRY & BIODIVERSITY
  • Masaaki Sugiyama
  • ,
  • Norihiko Fujii
  • ,
  • Yukio Morimoto
  • ,
  • Keiji Itoh
  • ,
  • Kazuhiro Mori
  • ,
  • Toshiharu Fukunaga
  • ,
  • Noriko Fujii

7
6
開始ページ
1380
終了ページ
1388
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/cbdv.200900332
出版者・発行元
WILEY-V C H VERLAG GMBH

Aggregation states of human alpha-crystallins are observed complementarily using small-angle X-ray and small-angle neutron scatterings (SAXS and SANS). Infant alpha-crystallin is almost a monodispersed system of the aggregates with gyration radius of ca. 60 angstrom, which is a normal aggregate. On the other hand, the aged and cataract alpha-crystallins have not only the normal but also the larger aggregates. In the aged alpha-crystallin, the normal aggregate is a major component, but in the cataract alpha-crystallin the larger ones are dominant. Both alpha A- and alpha B-crystallins, which are subunits of alpha-crystallin, also form an aggregate with the size close to the normal aggregate. Under UV irradiation, only aggregates of alpha B-crystallin undergo further aggregation. Therefore, considering increase of ratio of aB-crystallin in the aggregate of alpha-crystallin as aging, the abnormal aggregation (formation of the huge aggregates) mainly results in thefurther aggregation of alpha B-crystallin caused by external stresses.

リンク情報
DOI
https://doi.org/10.1002/cbdv.200900332
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/20564557
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000281310800007&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/cbdv.200900332
  • ISSN : 1612-1872
  • eISSN : 1612-1880
  • PubMed ID : 20564557
  • Web of Science ID : WOS:000281310800007

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