[Comparative study of bovine ocular lens proteins in native tissue and an extract using the x-ray diffraction method].
It has been shown that the maxima (Bragg-spacings 4,5-19 A) on the X-ray diffraction patterns of the bovine lens native tissues from nuclear and cortical parts are predominantly due to the water-soluble crystallin intramolecular structure. The structures of water-soluble and water-insoluble fractions from bovine lens nucleus and cortex were qualitatively compared. Reversible dependence of the lens water-soluble protein structure on water content in the system was demonstrated.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003459:Crystallins / Q000032:analysis*; D007903:Lens Capsule, Crystalline / Q000032:analysis; D007904:Lens Cortex, Crystalline / Q000032:analysis; D007908:Lens, Crystalline / Q000032:analysis*; D014020:Tissue Extracts / Q000032:analysis; D014961:X-Ray Diffraction
D003459:Crystallins; D014020:Tissue Extracts
Sravnitel'noe issledovanie belkov khrustalika glaza byka v nativnoĭ tkani i v ékstrakte metodom difraktsii rentgenovskikh lucheĭ.