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Structural Study on αA-Crystallin and βB2-crystallin Complex by Small-Angle X-ray Scattering
| Content Provider | Semantic Scholar |
|---|---|
| Author | Sugiyama, Masaaki Fujii, Norihiko Kawabe, Shunsuke Itoh, Keiji Mori, Kazuhiro Fukunaga, Toshiharu Fujii, Noriko |
| Copyright Year | 2009 |
| Abstract | Introduction Main optical functions of eye lens are high refractive index and high transparency. For former feature, there are high concentrated proteins, α-, β-, γ-crystallin, in eye lens. Among the proteins, α-crystallin with the largest molecular weight of ca 800 kDa has a chaperone activity to prevent from anomalous huge aggregation of the crystallins in the human eye lens. Therefore, it is considered that α-crystallin plays an important role to maintain the transparency. Recently, it is focused that protein aggregated deceases such as variant Creutzfeldt-Jakob disease (caused by abnormal prion), Alzheimer’s disease (caused by βamyloid proteins) and so on. The denatured protein makes the abnormal and huge aggregates: in the case of crystallin, the aggregated crystallin finally causes Catarct, which could be considered as one of protein aggregated deceases. Therefore, it is very important to reveal a repairing mechanism of α-crystallin. It is supposed that α-crystallin makes a complex with a denatured protein, for example denatured β-crystallin, when the α-crystallin fix the denatured protein. In order to observe making a complex with α-crystallin and the denatured protein, we adopt a small-angle X-ray scattering (SAXS). As the first step, we observe the solution with normal α-crystallin and normal β-crystallin. Here, we report the result of this preliminary experiment. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://pfwww.kek.jp/acr2008pdf/part_b/pf08b227.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
