Studies on extracellular ATP: Nucleotide pyrophosphotransferase from Streptomyces adephospholyticus. II. Purification and some properties of ATP: Nucleotide pyrophosphotransferase of Streptomyces adephospholyticus.

ATP: nucleotide pyrophosphotransferase was purified from culture filtrate of Streptomvices adephospholyticus A-4668 about 13, 000 fold by the method including ammonium sulfate fractionation, Amberlite IRC-50 treatment and column chromatography with DEAE-cellulose, DEAF-Sephadex A-25, SP-Sephadex C-25 and Sephadex G-75. The purified enzyme was homogenous on disk gel electrophoresis and ultracentrifugation and the specific activity was 915 units per mg protein. The molecular weight was determined as 28, 000 by gel filtration on Sephadex G-75. The enzyme was found to be stable in the pH range of 5.5 to 10.5. More than 80% of the activity was remained after heating at 60°C for 30min. The enzyme exhibited maximum activity at 50°C.