2001 Volume 65 Issue 10 Pages 2343-2346
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.
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