PARTIAL PURIFICATION AND CYTOTOXIC ACTIVITY OFL-ASPARAGINASE ISOLATED FROM Escherichia coli

Authors

  • Ayat Abbas Biotechnology Research Center, University of Al Nahrain. Baghdad-Iraq.
  • Majeed Sabbah Biotechnology Research Center, University of Al Nahrain. Baghdad-Iraq.
  • Omer Kathum Biotechnology Research Center, University of Al Nahrain. Baghdad-Iraq.

DOI:

https://doi.org/10.24996/ijs.2010.51.2.%25g

Keywords:

PARTIAL, CYTOTOXIC

Abstract

L-Asparaginase (E.C.3.5.1.1) is an important natural product that possesses a
broad spectrum of antitumor activity. In the present study, L-asparaginase partially
purified from local isolate of Escherichia coli that were grown aerobically for four
hours and anaerobically for 18hrs on M9 medium contain L-asparagine as sole
nitrogen source. Extraction of the enzyme was done by sonication. Qualitative and
quantitative assays for L-Asparaginase production were determined using
colorimetric and nesslerization methods respectively. The purification steps involve
dialysis of crude extract and DEAE-Cellulose Ion exchange chromatography. The
enzyme was purified 3.39-folds and showed a final specific activity of 0.18 U/mg
with a 41% yield. The crude extract and DEAE-Cellulose fractions showed slight
growth inhibition against RD cell line (human rhambdomyo sarcoma).

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Published

2024-09-06

Issue

Section

Biotechnology

How to Cite

[1]
A. . . Abbas, M. Sabbah, and O. . . Kathum, “PARTIAL PURIFICATION AND CYTOTOXIC ACTIVITY OFL-ASPARAGINASE ISOLATED FROM Escherichia coli”, Iraqi Journal of Science, vol. 51, no. 2, pp. 290–294, Sep. 2024, doi: 10.24996/ijs.2010.51.2.%g.

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