Crystallization and Properties of Aldolase from a Transplan table Rat Sarcoma1
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چکیده
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
منابع مشابه
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 homo...
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