ArticleThe open biochemistry journal2016
Purification, Characterization and Comparison between Two New L-asparaginases from
Article in The open biochemistry journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- The structural insights of L-asparaginase from3 Biotech · 2024Article
- Production of highly cytotoxic and low immunogenic L-asparaginase from Stenotrophomonas maltophilia EMCC2297.AMB Express · 2024Article
- Characterization of a Type II L-Asparaginase from the HalotolerantLife (Basel, Switzerland) · 2023Article
- Production and Anticancer Activity of an L-Asparaginase from Bacillus licheniformis Isolated from the Red Sea, Saudi Arabia.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundL-asparaginase has been used as a chemotherapeutic agent in treatment of lymphoblastic leukemia. In the present investigation,
methodsL- asparaginases were produced using different culture media and were purified using ion exchange chromatography.
resultsMaximum productivity was obtained when asparagine was used as the nitrogen source at pH 7 and 48 h after cultivation. New intracellular L-asparaginases showed an apparent molecular weight of 25 kDa and 30 kDa by SDS-PAGE respectively. These enzymes were active in a wide pH range (3-9) with maximum activity at pH 6 for
conclusionThe results revealed that both enzymes had appropriate characteristics and thus could be a potential candidate for medical applications.
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Registered trials
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