[A structural study of crystallins in the normal and cataractous crystalline lens by x-ray diffraction].

Nucleus of the normal and cataractous human lenses were studied by means of the X-ray diffraction method. The conformational changes, as it is shown, take place during cataract formation. The similar as in senile cataract, conformational changes of bovine lens crystallins were induced by UV irradiation.

[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.

[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.

[X-ray diffraction in the intact isolated frog ocular lens].

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.

[Comparative x-ray diffraction study of the crystalline lens in a number of vertebrates including man].

X-ray diffraction method has been applied for comparative investigation of native structure of eye lens proteins (crystallins). X-ray diffraction patterns of the whole lenses and/or their nuclear parts were obtained for man and vertebrate animals. Crystalline lenses of the fishes Acerina cernua and Pelmatochromis kribensis, frog Rana temporaria, bull and man contain crystallins with a very similar secondary and tertiary structure, whereas lenses of chicks and the tortoise Testudo horsfieldi contain mainly crystallins with other structure.

[Acute angle x-ray scattering by phospholipid membranes after treatment with valinomycin].

It has been found by means of small-angle X-ray analysis of oriented bilayers of synthetic dimyristoyl phosphatidyl choline that the introduction of valinomycin modifies their structure and these modifications depend on the phase state of lipid.

[Quaternary structure of histidine decarboxylase according to small-angle x-ray diffraction and electron microscopic findings].

The data on small angle X-ray scattering with histidine decarboxilase (HDC) from Micrococcus sp. n. were analysed and a line of succesively improving approximations of the molecule shape was found: by oblate ellipsoid a:b:c = 1:10.

[Determination of the molecular weight and form of the molecule histidine decarboxylase by the method of small-angle x-ray scattering].

Shape and molecular weight of histidine-decarboxylase from Micrococus sp. n. were studied by the method of X-ray small-angle scattering.