The specificity of horse liver alcohol dehydrogenase for cyclohexanol and its 3-methyl derivatives was investigated by stopped-flow and initial velocity kinetic studies. The (1S,3S)-3-methylcyclohexanol was 7 times more reactive (V/Km) than cyclohexanol, whereas the (1R,3R)-3-methylcyclohexanol was at least 1000 times less reactive than its enantiomer. Computer simulation of the transient reaction of NAD+ and the cyclohexanols catalyzed by the enzyme suggests that the rate of transfer of hydrogen from the alcohol to NAD+ is increased with the 1S,3S isomer. Modeling of the three-dimensional structure of the ternary complex of the enzyme suggests that the 1S,3S isomer should only bind in a productive, reactive mode, whereas the 1R,3R isomer would bind predominantly in a nonproductive, inhibitory mode.
Adequate anterior segment visualization during cataract surgery can be hindered when excessive tear film secretions precipitate on the corneal surface before the initial corneal incision is made. In most cases, room-temperature balanced salt solution applied to the corneal surface clears the debris. However, in cases in which tear film precipitates persist after the use of room-temperature balanced salt solution, the application of warm balanced salt solution can provide rapid and sustained dispersion of the precipitates. We present our experience using this technique.
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