Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules.
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.
Doremus
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Interdisciplinary Plant Physiology and Biochemistry Group, 204 Curtis Hall, University of Missouri-Columbia, Columbia, Missouri 65211.
Blevins
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