Expression and the refolding of a disulphide rich protein in a hydrophobic resin environment, bothropstoxin-I A Lys49-phospholipase 'A ind. 2' homologue (2001)
- Authors:
- USP affiliated authors: WARD, RICHARD JOHN - FFCLRP ; ROSA, JOSE CESAR - FMRP ; GREENE, LEWIS JOEL - FMRP
- Unidades: FFCLRP; FMRP
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
WARD, Richard John et al. Expression and the refolding of a disulphide rich protein in a hydrophobic resin environment, bothropstoxin-I A Lys49-phospholipase 'A ind. 2' homologue. 2001, Anais.. São Paulo: SBBq, 2001. . Acesso em: 25 abr. 2024. -
APA
Ward, R. J., Oliveira, A. H. C. de, Bortoleto, R. K., Rosa, J. C., Faça, V. M., & Greene, L. J. (2001). Expression and the refolding of a disulphide rich protein in a hydrophobic resin environment, bothropstoxin-I A Lys49-phospholipase 'A ind. 2' homologue. In Programa e Resumos. São Paulo: SBBq. -
NLM
Ward RJ, Oliveira AHC de, Bortoleto RK, Rosa JC, Faça VM, Greene LJ. Expression and the refolding of a disulphide rich protein in a hydrophobic resin environment, bothropstoxin-I A Lys49-phospholipase 'A ind. 2' homologue. Programa e Resumos. 2001 ;[citado 2024 abr. 25 ] -
Vancouver
Ward RJ, Oliveira AHC de, Bortoleto RK, Rosa JC, Faça VM, Greene LJ. Expression and the refolding of a disulphide rich protein in a hydrophobic resin environment, bothropstoxin-I A Lys49-phospholipase 'A ind. 2' homologue. Programa e Resumos. 2001 ;[citado 2024 abr. 25 ] - Structure/function studies of the G11-xylanase from Bacillus subtilis (1A1)
- Refolding and purification of Bothropstoxin-I, a Lys49-phospholipase 'A IND.2' homologue, expressed as inclusion bodies in Escherichia coli
- Expression, purification and crystallization of xylanase G11 from Bacillus subtilis
- Topology of the substrate-binding site of a 'Lys POT 49'-phospholipase 'A IND2' influences 'Ca POT 2+'-independent membrane-damaging activity
- Efficient constitutive expression of Bacillus subtilis xylanase A in Escherichia coli DH5'alfa' under the control of the Bacillus BsXA promotor
- Subproteomic analysis of soluble proteins of the microsomal fraction from two Leishmania species
- Expression in E. coli and purification of the nucleoside diphosphate kinase b from Leishmania major and site-directed mutagenesis of the active site region
- Targets for functional studies selected by subcellular proteome analysis of Leishmania major
- Targets for functional studies selected by subcellular proteome of Leishmania major
- Protein targets for structural studies selected by subcellular proteome of Leishmania major
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