BIOCHEMICAL CHARACTERIZATION, ANTIPROLIFERATIVE AND CYTOTOXICITY EFFECT OF PURIFIED L-ASPARAGINASE, AN ANTI-LEUKEMIA ENZYME ISOLATED FROM NEW BACTERIA Myroides Gitamensis

L-asparaginase (L-asp) is used in the treatment of acute lymphocytic leukemia (ALL). L-asp catalyzes the L-asp into ammonia and L-aspartic acid through deamination. The formed ammonia finds to be toxic to the organisms. Therefore, the search for less cytotoxic anti-proliferative L-asp is of great importance. Because of its cost-effectiveness, consistency, and easiness of process control, microbial L-asp is chosen over plant or animal enzymes. L-asp enzyme which was studied in the article was isolated from a newly discovered bacteria Myroides gitamensis. The biochemical characteristics and ant proliferative, the cytotoxic effect of purified L-asp was studied in order to develop safer biochemically stable anti-leukemia medication. To provide comprehensive information on the characteristics of the isolated L-asparaginase enzyme analytical tools were utilized, including cancer cell lines, brine shrimps, enzyme reactions, etc. MOLT-4 and K-562 cell lines showed an IC50 value of 91.41 IU/mL and 77.42 IU/mL, respectively. Cytotoxicity activity of L-asp on Artemia salina showed that at 24 hours (LC50 value of 217.0 µg/mL) and toxic at 48 hours (LC50 value of 126.4µg/ml)

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