Crystallization and properties of aldolase from a transplantable rat sarcoma.

Aldolase was isolated in a crystalline form in a 6% yield from rat Rhodamine sarcomas. The purification involved extraction with Tris-buffer, batchwise treatment with diethylaminoethylcellulose, ammonium sulfate fractionation, column chromatography on cellulose phosphate, and crystallization from ammonium sulfate solution (0.35 saturation). The crystalline aldolase preparation behaved as a homogeneous protein during electrophoresis and ultracentrifugai sedimentation. Aldolase of Rhodamine sarcoma was identical to aldolase A of normal rat muscle according to the following criteria: the crystalline aldolase had a specific activity of 12.5 units/mg protein; Km values were 4 X 10~s M for fructose 1,6-diphosphate and 1 X 10~2 M for fructose 1-phosphate; the activity for fructose