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Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) from chicken liver has been purified about 650 fold and crystallized. The crystalline enzyme was cube shaped and showed a specific activity of 46 units per mg of protein. The homogeneity of the crystalline enzyme was shown by polyacrylamide gel-disc electrophoresis. The sedimentation coefficient (s-degrees 2o,w) was 5.4 S. The crystalline enzyme was activated by the substrate inosine. The Hill coefficient was estimated to be 0.76, suggesting negative cooperativity with regard to the substrate inosine. The results of the kinetic analysis are consistent with the mechanism being a "rapid equilibrium random Bi-Bi reaction". The apparent equilibrium constant for phosphorolysis was 0.048.
K Murakami, and
K Tsushima
February 1969,
The Journal of biological chemistry,
K Murakami, and
K Tsushima
January 1978,
Methods in enzymology,
K Murakami, and
K Tsushima
January 2011,
Biomeditsinskaia khimiia,
K Murakami, and
K Tsushima
November 1971,
FEBS letters,
K Murakami, and
K Tsushima
February 1975,
European journal of biochemistry,
K Murakami, and
K Tsushima
January 1985,
Comparative biochemistry and physiology. B, Comparative biochemistry,
K Murakami, and
K Tsushima
January 2007,
Nucleosides, nucleotides & nucleic acids,
K Murakami, and
K Tsushima
January 1990,
Comparative biochemistry and physiology. B, Comparative biochemistry,
K Murakami, and
K Tsushima
November 1992,
Biochimica et biophysica acta,
K Murakami, and
K Tsushima
January 1978,
Methods in enzymology,
