[Study of the remote results of the use of repellants. Report 1. Experimental study of the long-term effects of the repellant diethyltoluamide (DETA)].
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Biomedical subjects
Publications and source records attributed to G M Nikolaev.
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Normal and cataractal decapsulated lenses of man were studied by NMR method-spin echo to obtain information concerning efficient coefficients of self diffusion, times of spin-spin relaxation of water protons (T2) and water content in the lens (c) at 25 degrees C in the course of cataractogenesis. It has been found that the values T2 and c at 25 degrees C are much higher in the nuclei of completely turbid lenses than in the transparent ones; the self-diffusion coefficients in the turbid lenses were also higher. At -9 degrees C a significant decrease of the content of undestroyed by frost (bound) water was observed at the stage of mature cataract as compared to transparent lenses. It is suggested that the most specific differences between the nuclei of transparent and completely turbid lenses are related to increased diffusion mobility of water molecules, apparently, at the expense of damaged plasmic membranes of the lens fibres noted during cataract development.
Water proton spin-spin relaxation times (T2) and the content of bound, "non-freezable" at -9 degrees C water in both normal human lenses and human lenses of different stages of cataract progression (cataracta incipiens, nondum matura, mature hypermatura) were measured by NMR spin echoes method. By the stage of cataracta nondum matura, increase of bound water content and simultaneous, almost half decrease of the relaxation time (T2), were observed. However, on the following stages of cataract evaluation (almost mature, mature cataracts) a gradual decrease of bound water content is noted, but only for the mature cataract stage the water content significantly differs from that of the normal one. On the stage of hypermature cataract the presence of two unexchanged with each other fractions of water is found. The obtained data are explained by lens protein reconstructions during the cataract progression.
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