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Updated: Jun 12, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
Published on: November 5, 2018
SAXS and SANS observations of abnormal aggregation of human alpha-crystallin
Masaaki Sugiyama1, Norihiko Fujii, Yukio Morimoto
1Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan.
Abstract:
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 A, 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 alpha B-crystallin in the aggregate of alpha-crystallin as aging, the abnormal aggregation (formation of the huge aggregates) mainly results in the further aggregation of alpha B-crystallin caused by external stresses.