Osmolytes stabilize L-asparaginase II without changing its secondary structure (2016)
- Authors:
- USP affiliated authors: PESSOA JUNIOR, ADALBERTO - FCF ; SOUZA, GISELE MONTEIRO DE - FCF
- Unidade: FCF
- Subjects: ENZIMAS; AMINOÁCIDOS
- Language: Inglês
- Imprenta:
- Source:
- Título: Brazilian Journal of Pharmaceutical Sciences
- ISSN: 1984-8250
- Volume/Número/Paginação/Ano: v. 52, suppl. 1, p. 29 res. FCF054, 2016
- Conference titles: Pharmaceutical Sciences and Technology Meeting of the Faculty of Pharmaceutical Sciences, University of São Paulo
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ABNT
WLODARCZYK, Samarina Rodrigues e PESSOA JUNIOR, Adalberto e MONTEIRO, Gisele. Osmolytes stabilize L-asparaginase II without changing its secondary structure. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo. . Acesso em: 14 mar. 2026. , 2016 -
APA
Wlodarczyk, S. R., Pessoa Junior, A., & Monteiro, G. (2016). Osmolytes stabilize L-asparaginase II without changing its secondary structure. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo. -
NLM
Wlodarczyk SR, Pessoa Junior A, Monteiro G. Osmolytes stabilize L-asparaginase II without changing its secondary structure. Brazilian Journal of Pharmaceutical Sciences. 2016 ; 52 29 res. FCF054.[citado 2026 mar. 14 ] -
Vancouver
Wlodarczyk SR, Pessoa Junior A, Monteiro G. Osmolytes stabilize L-asparaginase II without changing its secondary structure. Brazilian Journal of Pharmaceutical Sciences. 2016 ; 52 29 res. FCF054.[citado 2026 mar. 14 ] - Producing L-asparaginase of Erwinia chrysanthemi improved by synthetic evolution of proteins
- Engineered erwinase with possible fewer adverse effects for treatment of acute lymphoblastic leukemia
- Enzima da levedura do pão pode ser alternativa para tratar leucemia infantil
- Heterologous expression and purification of active L-Asparaginase I of Saccharomyces cerevisiae in Escherichia coli host
- Influence and effect of osmolytes in biopharmaceutical formulations
- Double mutant l-asparaginase of Erwinia chrysanthem which may have minor adverse effects
- Characterization of a new microbial ASNase with unique structural characteristics and high citotoxicity over acute lymphoblastic leukemia cells
- Fed-Batch Production of Saccharomyces cerevisiae L-Asparaginase II by Recombinant Pichia pastoris MUTs Strain
- Randomized and rational modifications of the Escherichia coli asparaginase aiming to enhance its effectiveness in the treatment of the lymphatic cancers
- Mutant L-asparaginase of Dickeya chrysanthemi (Erwinia chrysanthemi) with better biochemical parameters
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