Production of active L-asparaginase mutants by error-prone polymerase chain reactions (2015)
- Authors:
- USP affiliated authors: PESSOA JUNIOR, ADALBERTO - FCF ; SOUZA, GISELE MONTEIRO DE - FCF
- Unidade: FCF
- Subjects: ENZIMAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Brazilian Journal of Pharmaceutical Sciences
- ISSN: 1984-8250
- Volume/Número/Paginação/Ano: v. 51, suppl. 1, p. 40 res. FCF075, 2015
- Conference titles: Pharmaceutical Science and Technology Meeting of the Faculty of Pharmaceutical Sciences, University of São Paulo
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ABNT
RODRIGUES, Mariane Augusta Domingues et al. Production of active L-asparaginase mutants by error-prone polymerase chain reactions. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo. . Acesso em: 19 abr. 2024. , 2015 -
APA
Rodrigues, M. A. D., Leite, M. S. M., Pessoa Junior, A., & Monteiro, G. (2015). Production of active L-asparaginase mutants by error-prone polymerase chain reactions. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo. -
NLM
Rodrigues MAD, Leite MSM, Pessoa Junior A, Monteiro G. Production of active L-asparaginase mutants by error-prone polymerase chain reactions. Brazilian Journal of Pharmaceutical Sciences. 2015 ; 51 40 res. FCF075.[citado 2024 abr. 19 ] -
Vancouver
Rodrigues MAD, Leite MSM, Pessoa Junior A, Monteiro G. Production of active L-asparaginase mutants by error-prone polymerase chain reactions. Brazilian Journal of Pharmaceutical Sciences. 2015 ; 51 40 res. FCF075.[citado 2024 abr. 19 ] - Mutant L-asparaginase of Dickeya chrysanthemi (Erwinia chrysanthemi) with better biochemical parameters
- Functional and structural evaluation of the antileukaemic enzyme L-asparaginase II expressed at low temperature by different Escherichia coli strains
- Saccharomyces cerevisiae L-asparaginase 1: rational modifications aiming the modulation of kinetic characteristics over different substrates
- Producing L-asparaginase of Erwinia chrysanthemi improved by synthetic evolution of proteins
- Osmolytes stabilize L-asparaginase II without changing its secondary structure
- Evaluation of bacterial expression strains for the production of recombinant L-asparaginase, an antileukemic enzyme from Escherichia coli
- Evaluation of the activity and resistance to proteolytic cleavage of recombinat L-asparaginase obtained by error-prone polymerase chain reaction
- Enzima da levedura do pão pode ser alternativa para tratar leucemia infantil
- Effect of different osmolyte concentrations in the L-asparaginase II activity
- Influence and effect of osmolytes in biopharmaceutical formulations
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