Article3 Biotech2011
Cloning, expression and characterization of l-asparaginase from Withania somnifera L. for large scale production.
Article in 3 Biotech, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 64 citations in OpenAlex.
- l-Asparaginase fromACS omega · 2024Article
- L-Asparaginase fromPharmaceuticals (Basel, Switzerland) · 2022Article
- Development of Processes for Recombinant L-Asparaginase II Production byPharmaceutics · 2020Article
- Constitutive expression of Asparaginase in Gossypium hirsutum triggers insecticidal activity against Bemisia tabaci.Scientific reports · 2020Article
- Cloning and expression of L-asparaginase from Bacillus tequilensis PV9W and therapeutic efficacy of Solid Lipid Particle formulations against cancer.Scientific reports · 2018Article
- Purification, Characterization and Comparison between Two New L-asparaginases fromThe open biochemistry journal · 2016Article
- Cloning, expression and characterization of L-asparaginase from Pseudomonas fluorescens for large scale production in E. coli BL21.3 Biotech · 2015Article
- Biochemical characterization of a novel L-Asparaginase with low glutaminase activity from Rhizomucor miehei and its application in food safety and leukemia treatment.Applied and environmental microbiology · 2014Article
- Refolding and purification of recombinant L-asparaginase from inclusion bodies of E. coli into active tetrameric protein.Frontiers in microbiology · 2014Article
- Update on the Use of l-Asparaginase in Infants and Adolescent Patients with Acute Lymphoblastic Leukemia.Clinical Medicine Insights. Oncology · 2014Review
- Cloning, expression, purification and characterisation of Erwinia carotovora L-asparaginase in Escherichia coli.Advanced biomedical research · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
l-Asparaginase (E.C. 3.5.1.1) is used as a therapeutic agent in the treatment of acute childhood lymphoblastic leukemia. It is found in a variety of organisms such as microbes, plants and mammals. In plants, l-asparaginase enzymes are required to catalyze the release of ammonia from asparagine, which is the main nitrogen-relocation molecule in these organisms. An Indian medicinal plant, Withania somnifera was reported as a novel source of l-asparaginase. l-Asparaginase from W. somnifera was cloned and overexpressed in E. coli. The enzymatic properties of the recombinant enzyme were investigated and the kinetic parameters (K(m), k(cat)) for a number of substrates were determined. The kinetic parameters of selected substrates were determined at various pH and the pH- and temperature-dependence profiles were analyzed. WA gene successfully cloned into E. coli BL21 (DE3) showed high asparaginase activity with a specific activity of 17.3 IU/mg protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.