[Comparative study of crystallins from the nucleus and cortex of the bovine ocular lens by the gel filtration and x-ray diffraction methods].
Water--soluble proteins (alpha-, beta H-, beta L- and gamma-crystallins) from the bovine lens nucleus and cortex were fractionated and compared by gel filtration on Sephadex G-200. X-ray diffraction patterns from concentrated gels of these proteins were obtained. It allowed to compare qualitatively the structures of different crystallins and also to identify the maxima on X-ray diffraction patterns of the lens intact tissue.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000032:analysis*; D007904:Lens Cortex, Crystalline / Q000032:analysis*; D007907:Lens Nucleus, Crystalline / Q000032:analysis*; D007908:Lens, Crystalline / Q000032:analysis*; D014961:X-Ray Diffraction
D003459:Crystallins
Sravnitel'noe issledovanie kristallinov iadra i korteksa glaza byka metodami gel'-filtratsii i difraktsii rentgenovskikh lucheĭ.