Results 11 to 20 of about 11,907 (183)

Production, characterization, and antitumor efficiency of l-glutaminase from halophilic bacteria [PDF]

open access: yesBulletin of the National Research Centre, 2022
Background Halophiles are an excellent source of enzymes that are not only salt stable, but also can withstand and carry out reaction efficiently under extreme conditions.
Eman Zakaria Gomaa
doaj   +2 more sources

Evidence of Antioxidant Activity of Novel L-Glutaminase Purified from L. Gasseri BRLHM [PDF]

open access: yesJournal of Applied Sciences and Nanotechnology, 2021
Probiotic strains have the potential to be used as bio-preservatives and functional radical scavenging treatments in the future.  Antioxidant tests, including DPPH radical scavenging, were used to evaluate the antioxidant effects of extracellular L ...
Butheina Hasson, Likaa Mahdi, Rajwa Essa
doaj   +1 more source

Immunogenicity assessment of antileukemic agent glutaminase from Escherichia coli, Pseudomonas sp., and Bacillus sp.

open access: yesBiomedical and Biotechnology Research Journal, 2022
Background: L-glutaminase (L-glutaminase or glutamine amidohydrolase: EC 3.5.1.2) is an antileukemic agent which catalyzes the deamidation of glutamine to glutamic acid and ammonia.
Jyotsna Parmar   +2 more
doaj   +1 more source

Kinetic properties of Streptomyces canarius L- Glutaminase and its anticancer efficiency. [PDF]

open access: yesBraz J Microbiol, 2015
L-glutaminase was produced by Streptomyces canarius FR (KC460654) with an apparent molecular mass of 44 kDa. It has 17.9 purification fold with a final specific activity 132.2 U/mg proteins and 28% yield recovery. The purified L-glutaminase showed a maximal activity against L-glutamine when incubated at pH 8.0 at 40 °C for 30 min.
Reda FM.
europepmc   +6 more sources

Optimizing the Production of Glutaminase-Free L-Asparaginase by Halotolerant Penicillium sp. Isolated from Halophyte Cogongrass Rhizosphere [PDF]

open access: yesDelta Journal of Science, 2023
L-asparaginase is an enzyme included in the treatment of acute lymphoblastic leukemia (ALL). Its thrabiutic mechanism is the hydrolyzes of l-asparagine, which is essential amino acid for neoplastic cells while not essential and can be synthesized by ...
Abd El-Raheem El-Shanshoury   +2 more
doaj   +1 more source

In vitro Cytocidal Effect of L-Glutaminase on Leukaemic Lymphocytes [PDF]

open access: yesNature, 1971
MOUSE lymphomas, such as 6C3HED, undergo complete regression after one or more injections of L-asparaginase1, and remissions have been reported in some patients with acute leukaemia after treatment with L-asparaginase2–4. Roberts et al.5 found that purified bacterial L-glutaminase inhibited the growth of Ehrlich mouse carcinoma. Before considering this
R, Schrek   +3 more
openaire   +2 more sources

Bioprospecting of the agaricomycete Ganoderma australe GPC191 as novel source for l-asparaginase production

open access: yesScientific Reports, 2021
l-Asparaginase is a therapeutically and industrially-competent enzyme, acting predominantly as an anti-neoplastic and anti-cancerous agent. The existing formulations of prokaryotic l-asparaginase are often toxic and contain l-glutaminase and urease ...
Meghna Chakraborty, Srividya Shivakumar
doaj   +1 more source

In vivo stabilization of a less toxic asparaginase variant leads to a durable antitumor response in acute leukemia

open access: yesHaematologica, 2022
Asparagine is a non-essential amino acid since it can either be taken up via the diet or synthesized by asparagine synthetase. Acute lymphoblastic leukemia (ALL) cells do not express asparagine synthetase or express it only minimally, which makes them ...
Maaike Van Trimpont   +16 more
doaj   +1 more source

Metabolic Heterogeneity, Plasticity, and Adaptation to “Glutamine Addiction” in Cancer Cells: The Role of Glutaminase and the GTωA [Glutamine Transaminase—ω-Amidase (Glutaminase II)] Pathway

open access: yesBiology, 2023
Many cancers utilize l-glutamine as a major energy source. Often cited in the literature as “l-glutamine addiction”, this well-characterized pathway involves hydrolysis of l-glutamine by a glutaminase to l-glutamate, followed by oxidative deamination, or
Arthur J. L. Cooper   +3 more
doaj   +1 more source

Bioprospecting of Marine Fungi from Coastal Karnataka Region as Potential Source of Economically Important Enzyme L-Glutaminase and their Comparative Genomic Study

open access: yesJournal of Pure and Applied Microbiology, 2023
Marine fungi are important sources of new metabolites including certain enzymes of medical interest due to their enormous capacity to adapt themselves to extreme environments.
Sumangala Rao   +3 more
doaj   +1 more source

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