This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Roberts, J. Articles by Bachynsky, N. Search for Related Content PubMed PubMed Citation Articles by Roberts, J. Articles by Bachynsky, N.

The Antitumor Activity of Escherichia coli L-Asparaginase¹

Wadley Research Institute and Blood Bank and The Graduate Research Institute of Baylor University, Dallas, Texas

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.

¹ This publication was made possible through the support of the Leukemia Society, Inc.

Received 3/31/66.

This article has been cited by other articles:

				G. E. Jones and R. K. Mortimer L-Asparaginase-Deficient Mutants of Yeast Science, January 9, 1970; 167(3915): 181 - 182. [Abstract] [PDF]

				B. Horowitz, B. K. Madras, A. Meister, L. J. Old, E. A. Boyse, and E. Stockert Asparagine Synthetase Activity of Mouse Leukemias Science, May 3, 1968; 160(3827): 533 - 535. [Abstract] [PDF]