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The purification of phosphorylated form of rabbit liver glycogen phosphorylase (phosphorylase A) using the chromathography on a omega-amino-hexyl-Sepharose column has been carried out. The yield is about 90%, the specific activity is equal to 90 mkmol Pi/min. mg. The enzyme samples appeared essentially homogeneous when analyzed by polyacrylamide gel electrophoresis. The Km value of glucose-1-phosphate in the presence of AMP is 4--6 mM, which is higher than that found previously. When the glucose-1-phosphate concentration was varied, deviations from Michaelis-Menten kinetics were observed in the presence of glucose or ATP (Hill slopes of 1.6), but these deviations were virtually abolished by the presence of AMP. With glucose-1-phosphate as the substrate the Ki value of glucose is 57 mM in the absence of AMP and 150 mM in the presence of this effector. The Ki value of ATP is less dependent on the presence of AMP. The synergism in combined action of glucose and ATP has been revealed.
T B Eronina, and
G V Silonova, and
N B Livanova
September 1962,
The Journal of biological chemistry,
T B Eronina, and
G V Silonova, and
N B Livanova
October 1975,
The Journal of biological chemistry,
T B Eronina, and
G V Silonova, and
N B Livanova
May 1970,
The Journal of biological chemistry,
T B Eronina, and
G V Silonova, and
N B Livanova
March 1976,
Biochemistry,
T B Eronina, and
G V Silonova, and
N B Livanova
January 1990,
Biokhimiia (Moscow, Russia),
T B Eronina, and
G V Silonova, and
N B Livanova
July 1971,
Biochimica et biophysica acta,
T B Eronina, and
G V Silonova, and
N B Livanova
September 1968,
Archives of biochemistry and biophysics,
T B Eronina, and
G V Silonova, and
N B Livanova
January 1973,
Archives of biochemistry and biophysics,
T B Eronina, and
G V Silonova, and
N B Livanova
November 1977,
Biochemistry,
T B Eronina, and
G V Silonova, and
N B Livanova
December 1976,
The Biochemical journal,
