Erythrocytic Nucleoside Diphosphokinase

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Erythrocytic Nucleoside Diphosphokinase

Nucleoside diphosphokinase (NDP kinase) was identified in high concentrations in human erythrocytes, and a procedure was developed for the isolation of this enzyme. The best preparations had about 1400-fold greater specific activity (65 units per mg of protein) than that of hemolysates. Like crystalline yeast NDP kinase and partially purified NDP kinase preparations from various tissues, the er...

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Erythrocytic Nucleoside Diphosphokinase

Nucleoside diphosphokinase (NDP kinase) was identified in high concentrations in human erythrocytes, and a procedure was developed for the isolation of this enzyme. The best preparations had about 1400-fold greater specific activity (65 units per mg of protein) than that of hemolysates. Like crystalline yeast NDP kinase and partially purified NDP kinase preparations from various tissues, the er...

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Nucleoside diphosphokinase of Salmonella typhimurium.

Nucleoside diphosphokinase from Salmonella typhimurium has been purified and characterized. In many respects, the enzyme is similar to those from higher organisms in that it has a broad speciCcity for both phosphate donor and recipient and that it functions via a ping-pong mechanism. The enzyme activity of cells is very high at all growth rates but decreases as growth rate increases. Evidence i...

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Nucleoside diphosphokinase activity associated with DNA polymerases.

Nucleoside diphosphokinase activity is present in highly purified preparations of DNA polymerase from Micrococcus luteus and Escherichia coli, and in a partially purified DNA polymerase from avian myeloblastosis virus. The activity is also observed in the protein fragment of molecular weight 76,000 that is produced by subtilisin cleavage of DNA polymerase I from E. coli. The NDP kinase activity...

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Purification and properties of Bacillus subtilis nucleoside diphosphokinase.

Bacillus subfilis nucleoside diphosphokinase was purified l,lOO-fold to apparent homogeneity (a single band upon disc gel electrophoresis). Gel filtration through Sephadex G-ZOO indicated an approximate molecular weight of 100,000. The corrected Michaelis constants for the various nucleoside triphosphate substrates ranged from 0.10 fll~ for GTP to 0.42 mM for CTP. Deoxyribonucleoside triphospha...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1971

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)77215-9