title: [X-ray diffraction in the intact isolated frog ocular lens].
abstract: X-ray diffraction method has been applied for investigating ocular lens native tissue of the frog. X-ray diffraction patterns of intact lenses, their nuclei and cortices are similar and contain a set of concentric diffuse diffraction maxima. The most intensive of these maxima corresponding to the Bragg-spacings of 14.6, 9.1 and 4.6 A are presumably associated with intramolecular structure of lens proteins--crystallins. Intensive small-angle X-ray scattering and diffraction patterns isotropy indicates unavailability of crystallin molecule ordering or orientation in the lens. The shift of 14.6 A maximum up to 12.8 A being the result of nuclei drying shows the necessity of aqueous surrounding for these protein native structure maintenance.
mesh_terms: D000818:Animals; D003459:Crystallins / Q000032:analysis*; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000032:analysis*; D011487:Protein Conformation; D011896:Rana temporaria; D014961:X-Ray Diffraction
chemical_list: D003459:Crystallins
vernacular_title: Difraktsiia rentgenovskikh lucheĭ na tselom izolirovannom khrustalike glaza liagushki.