Characterization of nucleoside diphosphate kinase from moderately halophilic eubacteria.
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.
Yonezawa
Y
Y
Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan.
Tokunaga
H
H
Ishibashi
M
M
Tokunaga
M
M
D000595:Amino Acid Sequence; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D020632:Halomonas / Q000201:enzymology*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000378:metabolism
D012965:Sodium Chloride; D009701:Nucleoside-Diphosphate Kinase