Cloning and sequencing lysozyme genes from Musca domestica (2003)
- Authors:
- USP affiliated authors: MARANA, SANDRO ROBERTO - IQ ; TERRA, CLELIA FERREIRA - IQ ; TERRA, WALTER RIBEIRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; LISOZIMAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
EFFIO, Pedro Chimoy et al. Cloning and sequencing lysozyme genes from Musca domestica. 2003, Anais.. São Paulo: SBBq, 2003. . Acesso em: 29 mar. 2024. -
APA
Effio, P. C., Marana, S. R., Ferreira, C., & Terra, W. R. (2003). Cloning and sequencing lysozyme genes from Musca domestica. In Programa e Resumos. São Paulo: SBBq. -
NLM
Effio PC, Marana SR, Ferreira C, Terra WR. Cloning and sequencing lysozyme genes from Musca domestica. Programa e Resumos. 2003 ;[citado 2024 mar. 29 ] -
Vancouver
Effio PC, Marana SR, Ferreira C, Terra WR. Cloning and sequencing lysozyme genes from Musca domestica. Programa e Resumos. 2003 ;[citado 2024 mar. 29 ] - Site-directed mutagenesis of amino acid residues involved in the determination of the pH optimum in a beta-glycosidase
- The interplay of processivity, substrate inhibition and a secondary substrate binding site of an insect exo-'beta'-1,3-glucanase
- Purification of site directed mutants of a 'beta'-glycosidase
- Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis
- Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica
- Site-directed mutagenesis of amino acid residues involved in the determination of the substrate specificity in a beta-glycosidase
- Papel da R97 e da Y331 na determinação do pH ótimo em uma beta-glicosidase
- The active site of a midgut trehalase from Tenebrio molitor larvae
- Subsite of trypsin active site favor catalysis or substrate binding
- Subsites of trypsin active site favor catalysis or substrate binding
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