Purification of a soluble monoisozyme of nucleoside diphosphate kinase from chick brain: exploitation of ionic characteristics.

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 mumol/min/mg at 25 degrees C (using thymidine diphosphate as the phosphate acceptor and ATP as the donor) and is demonstrated to be monoisozymic.