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Characterization of nucleoside diphosphate kinase from moderately halophilic eubacteria
Y Yonezawa1, H Tokunaga, M Ishibashi
1Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan.
Bioscience, Biotechnology, and Biochemistry
|January 5, 2002
Abstract:
Nucleoside diphosphate kinase was purified to apparent homogeneity from naturally isolated moderately halophilic eubacteria by ATP-agarose and phenyl-5PW column chromatographies. The molecular mass of this enzyme was 15 kDa by time-of-flight mass-spectrometry. This protein showed anomalous mobility on SDS-PAGE which is typical of a halophilic protein. It was stable and active over a wide range of salt concentrations, from 0 to 4.0 M NaCl.