Abstract
Dolichol kinase was demonstrated in the microsomal fraction of Ascaris suum and Onchocerca volvulus. The enzyme from nematodes exhibited specificity for CTP as phosphoryl donor and was found to be inhibited by the reaction product CDP. Enzyme activity was optimal at pH 7.4, in the temperature range between 30° and 37°C, and in the presence of 0.5% Triton X-100. In addition, the enzyme was found to depend on divalent cations for activity; Mg 2+ being more effective than Mn 2+ and Ca 2+. The dolichol kinase from both nematodes was shown to be independent of Ca 2+-calmodulin for activity. The apparent K m values for dolichol were determined to be 7.5 and 9.0 μg ml −1 for the enzyme from A. suum and O. volvulus, respectively. Those for CTP were estimated to be 0.85 and 0.75 mM, respectively.
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