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| Content Provider | Springer Nature Link |
|---|---|
| Author | Krivandin, A. V. |
| Copyright Year | 2009 |
| Abstract | Heat-induced structural transitions of crystallins in the eye lens tissue have been studied by small-angle X-ray scattering. It is shown that a short-time (∼1 min) incubation of the bovine lens tissue at a temperature of ∼60°C leads to a pronounced shift of the small-angle x-ray diffraction maximum due to the short-range order of α-crystallin oligomers. This shift indicates an increase in the molecular mass of α-crystallin oligomers. The results are evidence that, in the native surrounding and at the natural concentration of α-crystallin, heat-induced transition of α-crystallin quaternary structure takes place. Earlier, this transition of α-crystallin has been observed only in solutions and gels of this protein. The results confirm the identity of α-crystallin properties in vitro and in vivo. |
| Starting Page | 448 |
| Ending Page | 449 |
| Page Count | 2 |
| File Format | |
| ISSN | 00063509 |
| Journal | Biophysics |
| Volume Number | 54 |
| Issue Number | 4 |
| e-ISSN | 15556654 |
| Language | English |
| Publisher | SP MAIK Nauka/Interperiodica |
| Publisher Date | 2009-12-09 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | α-crystallin quaternary structure heat-induced structural transition small-angle x-ray scattering Biophysics and Biological Physics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biophysics |
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