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SAXS and SANS Observations of Abnormal Aggregation of Human α ‐Crystallin
Author(s) -
Sugiyama Masaaki,
Fujii Norihiko,
Morimoto Yukio,
Itoh Keiji,
Mori Kazuhiro,
Fukunaga Toshiharu,
Fujii Noriko
Publication year - 2010
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200900332
Subject(s) - crystallin , small angle x ray scattering , chemistry , radius of gyration , aggregate (composite) , protein aggregation , biophysics , crystallography , biochemistry , optics , nanotechnology , materials science , scattering , polymer , organic chemistry , physics , biology
Aggregation states of human α ‐crystallins are observed complementarily using small‐angle X‐ray and small‐angle neutron scatterings (SAXS and SANS). Infant α ‐crystallin is almost a monodispersed system of the aggregates with gyration radius of ca. 60 Å, which is a normal aggregate. On the other hand, the aged and cataract α ‐crystallins have not only the normal but also the larger aggregates. In the aged α ‐crystallin, the normal aggregate is a major component, but in the cataract α ‐crystallin the larger ones are dominant. Both α A‐ and α B‐crystallins, which are subunits of α ‐crystallin, also form an aggregate with the size close to the normal aggregate. Under UV irradiation, only aggregates of α B‐crystallin undergo further aggregation. Therefore, considering increase of ratio of α B‐crystallin in the aggregate of α ‐crystallin as aging, the abnormal aggregation (formation of the huge aggregates) mainly results in the further aggregation of α B‐crystallin caused by external stresses.