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- W2007087601 abstract "When cells of a marine bacterium were washed and suspended in 0.05 M MgCl 2 , no isocitric dehydrogenase could be demonstrated in the extract prepared, although all other tricarboxylic acid cycle enzymes had been shown to be present. Failure to detect the enzyme was traced to the presence of halide as the sole anion in the solution used to suspend the cells. Sulphate or phosphate salts gave rise to an active enzyme. These relations applied to extracts prepared by sonic treatment, alumina grinding, and lysis by versene and lysozyme. Evidence was obtained suggesting that halides fail to prevent the denaturation of the enzyme after its release from the cells. Tested under optimum conditions, the specific activity of isocitric dehydrogenase in the extract was found to be proportional to the ionic strength of the solution used to suspend the cells (maximum activity at 0.4 to 0.5 μ). In the presence of low concentrations of an anion giving rise to an active enzyme, halide salts were found capable of contributing to these ionic strength requirements. The addition of Mg ++ to the extract in the presence of a suitable anion at least doubled the storage life of the enzyme at 4 °C." @default.
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- W2007087601 date "1960-07-01" @default.
- W2007087601 modified "2023-09-25" @default.
- W2007087601 title "NUTRITION AND METABOLISM OF MARINE BACTERIA: IX. ION REQUIREMENTS FOR OBTAINING AND STABILIZING ISOCITRIC DEHYDROGENASE FROM A MARINE BACTERIUM" @default.
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- W2007087601 doi "https://doi.org/10.1139/o60-086" @default.
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