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

Holly Doremus | Zendy; Dale G. Blevins | Zendy

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

Author(s) -

Holly Doremus,

Dale G. Blevins

Publication year - 1988

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.87.1.41

Subject(s) - nucleotide , nucleoside , biochemistry , enzyme , glycine , divalent , chemistry , hydrolysis , enzyme assay , specific activity , in vivo , biology , gene , amino acid , genetics , organic chemistry

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.

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