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Protein Expr Purif. 2003 Feb;27(2):195-201.

Purification and characterization of the deoxynucleoside monophosphate kinase of bacteriophage T5.

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Pushchino Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, ave Nauki 6, Pushchino, Moscow region 142290, Russia.


Deoxynucleoside monophosphate kinase (dNMP kinase) of bacteriophage T5 (EC was purified to apparent homogeneity from phage-infected Escherichia coli cells. Electrophoresis in sodium dodecyl sulfate-polyacrylamide gel showed that the enzyme has a molecular mass of about 29 kDa. The molecular mass of dNMP kinase estimated by analytical equilibrium ultracentrifugation turned out to be 29.14 +/- 3.03 kDa. These data suggest that the enzyme exists in solution as a monomer. The isoelectric point of dNMP kinase was found to be 4.2. The N-terminal amino acid sequence, comprising 21 amino acids, was determined to be VLVGLHGEAGSGKDGVAKLII. A comparison of this amino acid sequence and those of known enzymes with a similar function suggests the presence of a nucleotide-binding site in the sequenced region.

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