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The antitumor activity of Escherichia coli L-asparaginase.

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1966

Year

Abstract

Summary Two l-asparaginase components were isolated from Escherichia coli by diethylaminoethyl cellulose column chromatography. The early emerging component (Peak I l-asparaginase), capable of causing complete regression of the Gardner 6C3HED lymphosarcoma, exhibited optimum activity at pH 7.5–8.6 and was stable on prolonged incubation with C3H mouse serum or peritoneal ascitic fluid. In contrast, the Peak II l-asparaginase component exhibited optimum activity at about pH 8.5, was significantly inactivated on incubation with the mouse humoral fluids, and lacked tumor-inhibitory activity. A number of factors which may influence the therapeutic usefulness of enzymes are presented.