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WJPR Citation
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| All | Since 2020 | |
| Citation | 8502 | 4519 |
| h-index | 30 | 23 |
| i10-index | 227 | 96 |
PURIFICATION AND CHARACTERIZATION OF L-ASPARGINASE ENZYME FROM SPINACEA OLERACEA
Sarina P. Khabade*
Abstract L-asparaginase (E. C. 3.5.1.1) is an anticancer enzyme used as a drug to treat acute lymphoblastic leukaemia. In the present piece of work, Lasparaginase was purified from Spinacea oleraceae. The Lasparaginase enzyme was purified by salt precipitation (70%) followed by dialysis, anion exchange chromatography (DEAE- Cellulose) and gel filtration (sephadex G75) with final yield of 47.4% and purification fold 20.30. The molecular mass was found to be 160kda as estimated by SDS-PAGE. The enzyme activity of purified sample was found to be 322.3 IU and specific activity 1587.6μmoles/mg/min. This study aimed to determine novel source of L-asparaginase enzyme from Spinacea oleraceae, a possible solution for blood cancer. Keywords: L-asparaginase enzyme, Spinacea oleraceae, acute lymphoblastic leukaemia. [Full Text Article] [Download Certificate] |
