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Partial purification and characterization of NAD kinase from potato tuber

Partial purification and characterization of NAD kinase from potato tuber

Journal of the Faculty of Agriculture, Hokkaido University 58(4): 575-582

NAD kinase from tubers of potato Irish Cobbler was purified by >200 times. The enzyme had a single reaction band with polyacrylamide gel electrophoresis; its mol. wt. was 175 000. The enzyme was highly specific for NADP synthesis from NAD and ATP with the opt. pH 6.5-6.9. The Km values for NAD and ATP were 1.0 and 1.2 mM, resp. Ki values for NADH and NADPH (competitive inhibitors with respect to NAD) were 0.06 and 0.05 mM, resp.

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