Regulation of malate dehydrogenase from an osmoconformer by salt
In: Comparative biochemistry and physiology. B, Jg. 53 (1976), Heft 2
Online
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Zugriff:
1. 1. Malate dehydrogenase of the American oyster, Crassostrea virginiana, was partially purified. 2. 2. When reacted at various buffer concentrations, the enzyme demonstrated only a slight increase in catalytic activity at 80 mM potassium phosphate buffer. 3. 3. The apparent Michaelis Constants for NADH and for OAA were increased about 3-fold by increased concentration of buffer. 4. 4. Catalytic activity of oyster MDH was inhibited equally by high concentrations of OAA irrespective of ionic strength. 5. 5. The eco-adaptive implications of these observations are discussed.
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Regulation of malate dehydrogenase from an osmoconformer by salt
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Autor/in / Beteiligte Person: | Gomolinski, Eva ; Sarkissian, Igor V. |
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Zeitschrift: | Comparative biochemistry and physiology. B, Jg. 53 (1976), Heft 2 |
Veröffentlichung: | 1976 |
Medientyp: | unknown |
ISSN: | 0305-0491 (print) |
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