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Phosphoenolpyruvate Carboxykinase from Bakers' Yeast

ISOLATION OF THE ENZYME AND STUDY OF ITS PHYSICAL PROPERTIES

From the ¹ From the Cátedra de Química Biológica, Facultad de Medicina, Buenos Aires, Argentina

A modified purification procedure for phosphoenolpyruvate carboxykinase from bakers' yeast is described, which gives rise to enzyme in crystalline form. The isolated enzyme, after 1100-fold purification in a 6% yield, was found to be homogeneous by ultracentrifugal criteria. The following physical parameters of the enzyme were established: sedimentation coefficient (s⁰_20,w), 9.89 S; diffusion coefficient (d_20,w) (from boundary spreading during velocity sedimentation), 3.69 x 10^-7 cm² sec^-1, (d_20,w) (from molecular sieve analysis), 3.75 x 10^-7 cm² sec^-1; Stokes' radius (a), 57.0 A; partial specific volume (V), 0.735 ml g^-1; molecular weight, 252,000 g mole^-1; and frictional ratio (f/f₀), 1.36. The amino acid composition of the enzyme is reported.

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