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Metabolism and Enzymology

Purification and Characterization of a Specific Nucleoside Diphosphatase from Soybean Root Nodules ¹

Interdisciplinary Plant Physiology and Biochemistry Group, 204 Curtis Hall, University of Missouri-Columbia, Columbia, Missouri 65211

A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.

¹ Supported by the Missouri Agricultural Experiment Station and by a grant from the United States Department of Agriculture, Science and Education Administration, Competitive Grants Office, Grant 85-CRCR-1-1638. This research is a contribution of the Missouri Agricultural Experiment Station Journal Series No. 10412.