Pressure Regulation of Malic Dehydrogenase in Reversed Micelles
Malic dehydrogenase (MDH) studied in water and reversed micelles upon pressure application revealed a difference in catalysis. Whereas MDH in water appeared to be not sensitive to the pressure increasing, the catalytic activity of MDH in reversed micelles showed bell-shaped dependencies both on pres...
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Veröffentlicht in: | Biochemical and biophysical research communications 1999-01, Vol.254 (3), p.685-688 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Malic dehydrogenase (MDH) studied in water and reversed micelles upon pressure application revealed a difference in catalysis. Whereas MDH in water appeared to be not sensitive to the pressure increasing, the catalytic activity of MDH in reversed micelles showed bell-shaped dependencies both on pressure and surfactant hydration degree, w0. The catalytic activity of MDH was found to be maximal under moderate pressure equal to 300-500 bar and at w0approximately 14 with the difference between lowest and highest levels of the catalytic activity amounted to about 10 times. The work presented demonstrates for the first time the co-operative effect of reversed micelles and pressure application to malic dehydrogenase leading to the enzyme regulation that cannot be realized in aqueous solution. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1006/bbrc.1998.9993 |