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Дата издания
01.04.2022Область исследования
Тип исследования
Аннотация (краткое описание)
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 organism. Therefore, the search for less cytotoxic anti-proliferative L-asp is of great importance. Because of its costeffectiveness, consistency, and easiness of process control, microbial L-asparaginase 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 antiproliferative, cytotoxic effect of purified L-asp were 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). © 2022, Rasayan Journal of Chemistry, c/o Dr. Pratima Sharma. All rights reserved.DOI
10.31788/RJC.2022.1526842Тип публикаций
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