[Heat-induced structural transition of alpha-crystallin in the eye lens tissue observed by small-angle X-ray scattering].
Heat-induced structural transitions of crystallins in the eye lens tissue have been studied by small-angle X-ray scattering. It was shown that a short-time (approximately 1 min) incubation of the bovine eye lens tissue at a temperature of about 60 degrees C leads to a pronounced shift of the small-angle X-ray diffraction maximum due to the short-range order of alpha-crystallin oligomers. This shift indicates an increase in the molecular mass of alpha-crystallin oligomers. The results are evidence that, in the native surrounding and at the native concentration of alpha-crystallin, heat-induced transition of alpha-crystallin quaternary structure takes place. Earlier, this transition of alpha-crystallin has been observed only in solutions and gels of this protein. The results confirm the identity of alpha-crystallin properties in vitro and in vivo.
Krivandin
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D000818:Animals; D002417:Cattle; D006358:Hot Temperature; D007908:Lens, Crystalline / Q000737:chemistry*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012542:Scattering, Radiation; D014965:X-Rays; D038201:alpha-Crystallins / Q000737:chemistry*
D038201:alpha-Crystallins