Nucleosidetriphosphate: Nucleosidediphosphate Phosphotransferase (NTP-NDP Kinase) of Rhodospirillum rubrum: Its Purification and Properties
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1. From Rhodospirillum rubrum has been purified in a homogeneous purity nucleosidetriphosphate : nucleosidediphosphate phosphotransferase (the trivial name, NTP-NDP kinase), previously called ADP-ATP exchange enzyme. It has a molecular weight of approximately 30, 000 and an isoelectric point of 4.9.2. In the light-grown cells, most of NTP-NDP kinase was present in the cytoplasmic fluid, and the remainder was associated with chromatophore membrane. Chromatophores, if washed sufficiently, showed practically no activity of the enzyme. However, by sonication of the well-washed chromatophores the enzyme was solubilized; the increase of the activity was in parallel with the decrease of the activities of ATP hydrolysis, ATP-Pi exchange and photosynthetic ATP formation.3. All the nucleoside triphosphates and diphosphates tested served as the substrates of the purified enzyme. Of the triphosphates, ATP was most effective; the efficiencies relative to that of ATP was 57% for GTP, 41% for ITP, 24% for DTP, and 4% for CTP. Of the diphosphates, ADP, dADP, GDP, dGDP, UDP, dUDP, and IDP were similar in efficiency, whereas CDP and dCDP were 49% and 29%, respectively, in efficiency relative to that of ADP.4. The purified enzyme required cations for the activity. Of the cations tested, Mg2+ was most effective.5. The purified enzyme could be chemically combined with Sepharose. The enzyme-Sepharose complex, insoluble in water, showed the same activity as that of the free enzyme. By means of chromatography on a column of the enzyme-Sepharose complex, it was found that on reaction with ATP, the enzyme was phosphorylated and the phosphoryl enzyme produced radioactive ATP on reaction with radioactive ADP.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
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