Cloning and expression of recombinant biopharmaceutical prospective L-asparaginase from Saccharomyces cerevisae with ELP-intein tail (2015)
- Authors:
- USP affiliated authors: PESSOA JUNIOR, ADALBERTO - FCF ; SOUZA, GISELE MONTEIRO DE - FCF
- Unidade: FCF
- Subjects: SACCHAROMYCES; NEOPLASIAS; ENZIMAS; BIOTECNOLOGIA
- Language: Inglês
- Imprenta:
- Publisher: Pró-Reitoria de Pesquisa/USP
- Publisher place: São Paulo
- Date published: 2015
- Source:
- Título do periódico: Resumos
- Conference titles: Simpósio Internacional de Iniciação Científica e Tecnológica da USP (SIICUSP)
-
ABNT
BIASOTO, Henrique Pellin et al. Cloning and expression of recombinant biopharmaceutical prospective L-asparaginase from Saccharomyces cerevisae with ELP-intein tail. 2015, Anais.. São Paulo: Pró-Reitoria de Pesquisa/USP, 2015. . Acesso em: 23 abr. 2024. -
APA
Biasoto, H. P., Pimenta, M. V., Pessoa Junior, A., & Monteiro, G. (2015). Cloning and expression of recombinant biopharmaceutical prospective L-asparaginase from Saccharomyces cerevisae with ELP-intein tail. In Resumos. São Paulo: Pró-Reitoria de Pesquisa/USP. -
NLM
Biasoto HP, Pimenta MV, Pessoa Junior A, Monteiro G. Cloning and expression of recombinant biopharmaceutical prospective L-asparaginase from Saccharomyces cerevisae with ELP-intein tail. Resumos. 2015 ;[citado 2024 abr. 23 ] -
Vancouver
Biasoto HP, Pimenta MV, Pessoa Junior A, Monteiro G. Cloning and expression of recombinant biopharmaceutical prospective L-asparaginase from Saccharomyces cerevisae with ELP-intein tail. Resumos. 2015 ;[citado 2024 abr. 23 ] - 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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