A rapid and convenient method was developed for the measurement of the enzyme activity catalyzing the transphosphorylation reaction between a nucleoside diphosphate and a nucleoside triphosphate. With use of this method, a nucleoside diphosphokinase was purified 2800-fold from calf thymus and the purified enzyme was characterized with respect to substrate specificity, metal ion requirement, pH optimum, and kinetic constants. All nucleoside di- and triphosphates related to nucleic acids were found to be active as phosphate acceptors and donors, respectively. The purified preparation contained two forms of enzyme which differ significantly from each other in their chromatographic behavior on diethylaminoethyl cellulose.
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Nakamura et al. (1966) studied this question.
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