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- W1974937209 abstract "The elucidation of the mechanism of enzyme action generally requires knowledge of the maximum values of the thermodynamic parameters. High hydrostatic pressure associated with temperature variation can lead to such data. In this laboratory, the development of cryoenzymology, which mainly slows down reaction velocity, has permitted a description of catalytic cycles over a single turnover to isolate intermediates in order to analyze single steps. This thermal control of a reaction has opened the way for the investigation of the activation volume (ΔV≠) of each step and then to detect their stereochemical changes. This is experimentally attained using a specially designed stopped-flow apparatus interfaced to spectrophotometers working over a wide temperature range (+30 to −30°C in hydroorganic media) from 1 to 2000 bar. A description of the apparatus is given together with potential applications." @default.
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- W1974937209 date "1986-05-01" @default.
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- W1974937209 title "The application of high-pressure stopped-flow spectroscopy at low temperatures for the study of enzyme catalyzed reactions" @default.
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- W1974937209 doi "https://doi.org/10.1016/0378-4363(86)90720-5" @default.
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