Production of l -Asparaginase II by Escherichia coli

Author:

Cedar Howard1,Schwartz James H.1

Affiliation:

1. Department of Microbiology, New York University School of Medicine, New York, New York 10016

Abstract

l -Asparaginase II was synthesized at constant rates by Escherichia coli under anaerobic conditions. The enzyme was produced optimally by bacteria grown between p H 7 and 8 at 37 C. Although some enzyme was formed aerobically, between 100 and 1,000 times more asparaginase II was produced during anaerobic growth in media enriched with high concentrations of a variety of amino acids. Bacteria grown under these conditions should provide a rich starting material for the large-scale production of the enzyme. No single amino acid specifically induced the synthesis of the asparaginase, nor did l -asparagine, even when it was used as the only source of nitrogen. The enzyme was produced at lower rates in the presence of sugars; glucose was the most inhibitory.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference30 articles.

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3. Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. I. Properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance;Broome J. D.;J. Exptl. Med.,1963

4. Studies on the mechanism of tumor inhibition by L-asparaginase. Effects of the enzyme on asparagine levels in the blood, normal tissues, and 6C3HED Iymphomas of mice: differences in asparagine formation and utilization in asparaginase sensitive and resistent Iymphoma cells;Broome J. D.;J. Exptl. Med.,1968

5. Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity;Campbell H. A.;Biochemistry,1967

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