The active site of a midgut trehalase from Tenebrio molitor larvae (2005)
- Authors:
- USP affiliated authors: MARANA, SANDRO ROBERTO - IQ ; TERRA, WALTER RIBEIRO - IQ ; TERRA, CLELIA FERREIRA - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; COLEOPTERA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programas e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
GOMEZ, Ana et al. The active site of a midgut trehalase from Tenebrio molitor larvae. 2005, Anais.. São Paulo: SBBq, 2005. . Acesso em: 19 abr. 2024. -
APA
Gomez, A., Marana, S. R., Terra, W. R., & Ferreira, C. (2005). The active site of a midgut trehalase from Tenebrio molitor larvae. In Programas e Resumos. São Paulo: SBBq. -
NLM
Gomez A, Marana SR, Terra WR, Ferreira C. The active site of a midgut trehalase from Tenebrio molitor larvae. Programas e Resumos. 2005 ;[citado 2024 abr. 19 ] -
Vancouver
Gomez A, Marana SR, Terra WR, Ferreira C. The active site of a midgut trehalase from Tenebrio molitor larvae. Programas e Resumos. 2005 ;[citado 2024 abr. 19 ] - 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 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
- 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
- Subsite of trypsin active site favor catalysis or substrate binding
- Subsites of trypsin active site favor catalysis or substrate binding
- Expression, purification and crystallization of a recombinant digestive lysozyme from Musca domestica (diptera - insecta)
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