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Crystallization and Properties of Aldolase from a Transplantable Rat Sarcoma¹

Biochemistry Division, National Cancer Center Research Institute, Chuo-ko, Tokyo, Japan

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 diethylaminoethyl-cellulose, 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 ultracentrifugal 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; K_m values were 4 x 10^-5 M for fructose 1,6-diphosphate and 1 x 10^-2 M for fructose 1-phosphate; the activity for fructose 1,6-diphosphate was depressed to 6% of the original by carboxypeptidase A and inhibited completely by anti-aldolase A antibody but not at all by anti-aldolase B antibody; the fructose 1,6-diphosphate activity was inhibited by adenine nucleotides, most etficiently by adenosine triphosphate and less by adenosine diphosphate and adenosine monophosphate.

¹ This work was partly supported by Grants No. 9179 from the Ministry of Education and No. 4 from the Ministry of Health of Japan

Received 1/21/69. Accepted 3/18/69.