Abstract
A procedure for the rapid purification of nucleoside diphosphate kinase, 24 h with a single operator, from the chick brain soluble fraction is described. The influence of the ionic conditions on the association-disassociation properties of the enzyme are exploited to obtain yields of 30% from the crude homogenate. The enzyme has been purified 500-fold with a maximal specific activity of 1500 μmol/min/mg at 25°C (using thymidine diphosphate as the phosphate acceptor and ATP as the donor) and is demonstrated to be monoisozymic.
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