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l asparagine/hypersensitivity
Врската е зачувана во таблата со исечоци
Страница 1 од 18 резултати
The anti-asparagines antibodies correlate with L-asparagines activity and may affect clinical outcome of childhood acute lymphoblastic leukemia.
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The primary aim of the study was to evaluate the importance of anti-asparaginase antibodies for l-asparaginase activity in children with standard and medium risk acute lymphoblastic leukemia (ALL). Forty-seven children with newly diagnosed ALL were included into the prospective study. Enzyme
Characterization of polyethylene glycol-modified L-asparaginase from Escherichia coli and its application to therapy of leukemia.
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For the purpose of clinical application to the therapy of human leukemia and lymphosarcoma, L-asparaginase from Escherichia coli was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2) by an improved method, which involves a purification step of activated PEG2 by
A comprehensive review on microbial L-asparaginase: Bioprocessing, characterization and industrial applications.
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L-asparaginase (E.C.3.5.1.1.) is a vital enzyme which hydrolyzes L-asparagine to L-aspartic acid and ammonia. This property of L-asparaginase inhibits the protein synthesis in cancer cells, making L-asparaginase a mainstay of pediatric chemotherapy practices to treat acute lymphoblastic leukemia
Pharmacology, immunogenicity, and efficacy of a novel pegylated recombinant Erwinia chrysanthemi-derived L-asparaginase.
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Bacterial L-asparaginase (ASNase), hydrolyzing L-asparagine (Asn), is an indispensable component used in the treatment of acute lymphoblastic leukemia (ALL) and certain lymphoma entities. Native Erwinia chrysanthemi-derived ASNase (n-crisantaspase) has been approved as a second-line drug for
Individualized Asparaginase Dosing in Childhood Acute Lymphoblastic Leukemia.
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PURPOSE
In the DCOG ALL-11 protocol, polyethylene glycol-conjugated Escherichia coli asparaginase (PEGasparaginase) and Erwinia asparaginase treatment of pediatric acute lymphoblastic leukemia are individualized with therapeutic drug monitoring (TDM). The efficacySynthesis, characterization and immunogenicity of silk fibroin-L-asparaginase bioconjugates.
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L-asparaginase (ASNase) is one basic drug in the treatment of acute lymphoblastic leukemia (ALL). Because its half-life time is too short and it is easy to arouse allergic reaction, use in practical clinic is considerably limited. Silk fibroin (SF) with different molecular mass from 40 to 120 kDa is
Plasma asparaginase activity, asparagine concentration, and toxicity after administration of Erwinia asparaginase in children and young adults with acute lymphoblastic leukemia: Phase I/II clinical trial in Japan.
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BACKGROUND
A phase I/II study of Erwinia asparaginase in Japanese children and young adults with acute lymphoblastic leukemia (ALL) was performed to investigate its activity and toxicity.
METHODS
Eligible patients were in remission and had developed allergy to Escherichia coli asparaginase. Erwina
Evaluation of L-asparaginase: polyethylene glycol conjugate versus native L-asparaginase combined with chemotherapy. A randomized double-blind study in canine lymphoma.
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L-asparaginase is an enzyme that inhibits protein synthesis by the depletion of sources of L-asparagine, which is necessary for transformed lymphoid cells to proliferate. L-asparaginase is used in the treatment of childhood acute lymphoblastic leukemia. A problem with L-asparaginase therapy is the
[Significance of L-asparaginase activity and biochemical parameters evaluation in children with acute lymphoblastic leukemia].
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L-asparaginase is one of the most important agent used in multidrug chemotherapy regimens in the treatment of malignancies which derive from lymphoid system (acute lymhoblastic leukemias and non-hodgkin lymphoma). L-asparaginase leads to enzymatic cleavage of L-asparagine (amino acid essential for
Bacterial l-asparaginases for cancer therapy: Current knowledge and future perspectives.
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l-Asparaginases hydrolyzing plasma l-asparagine and l-glutamine has attracted tremendous attention in recent years owing to remarkable anticancer properties. This enzyme is efficiently used for acute lymphoblastic leukemia (ALL) and lymphosarcoma and emerged against ALL in children, neoplasia, and
A phase I and pharmacodynamic evaluation of polyethylene glycol-conjugated L-asparaginase in patients with advanced solid tumors.
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OBJECTIVE
To evaluate the in vitro activity of polyethylene glycol-conjugated L-asparaginase (PEG-Lasparaginase) against fresh human tumor specimens, using the human tumor clonogenic assay (HTCA), and to perform a phase I dose-escalation clinical trial of PEG-L-asparaginase. The goal of the clinical
Pegaspargase.
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L-asparaginase is an antineoplastic agent proven to be effective in depleting the amino acid L-asparagine in patients with childhood and adult acute lymphoblastic leukemia. It has become a significant part of most chemotherapy protocols, however, its use is sometimes limited by the development of
Monolith and coating enzymatic microreactors of L-asparaginase: kinetics study by MCE-LIF for potential application in acute lymphoblastic leukemia (ALL) treatment.
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The study of enzyme immobilization using an extracorporeal shunt system is essential to eliminate the side effects of L-asparaginase (L-Asnase; including hepatic toxicity, allergic reaction, pancreatitis, central nervous system toxicity and decreased synthesis of blood clotting factors) when it was
Therapeutic l-asparaginase: upstream, downstream and beyond.
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l-asparaginase (l-asparagine amino hydrolase, E.C.3.5.1.1) is an enzyme clinically accepted as an antitumor agent to treat acute lymphoblastic leukemia and lymphosarcoma. It catalyzes l-asparagine (Asn) hydrolysis to l-aspartate and ammonia, and Asn effective depletion results in cytotoxicity to
L-asparaginase: an effective agent in the treatment of acute lymphoblastic leukemia.
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L-asparaginase (L-ASNase) is an enzyme used most effectively in the treatment of acute lymphoblastic leukemia (ALL) for more than 30 years. It catalyzes the hydrolysis of amino acid l-asparagine to aspartic acid and ammonia, which leads to cell death. Clinical trials have been conducted using
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