Your browser doesn't support javascript.
loading
Cloning, expression and charaterization of chalcone synthase from Saussurea medusa / 生物工程学报
Chinese Journal of Biotechnology ; (12): 1363-1370, 2011.
Artigo em Chinês | WPRIM | ID: wpr-304567
ABSTRACT
A fragment of chalcone synthase gene (SmCHS) was cloned from the cDNA library constructed in Saussurea medusa. The full-length cDNA sequence of SmCHS was obtained by RT-PCR. Sequence analysis showed that the full length of SmCHS was 1313 bp, containing an open reading frame (1170 bp) encoding 389 amino acids. The molecular weight of the protein was estimated to be 43 kDa. The prokaryotic expression plasmids pET28a(+)-SmCHS was constructed and transformed into Escherichia coli BL21(DE3) for expression. SDS-PAGE indicated that the fusion protein was expressed partially in soluble form after induction by IPTG. The recombinant protein was collected and purified by Ni-NTA affinity column. The enzymatic activity assay of the purified recombinant protein showed that the fusion protein had chalcone synthase activity. It could catalyze the condensation of a 4-coumaroyl-CoA with three malonyl-CoAs to produce naringenin chalcone.
Assuntos
Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Proteínas de Plantas / Proteínas Recombinantes / Aciltransferases / Dados de Sequência Molecular / Catálise / Sequência de Aminoácidos / Clonagem Molecular / DNA Complementar / Saussurea / Chalconas Idioma: Chinês Revista: Chinese Journal of Biotechnology Ano de publicação: 2011 Tipo de documento: Artigo

Similares

MEDLINE

...
LILACS

LIS

Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Proteínas de Plantas / Proteínas Recombinantes / Aciltransferases / Dados de Sequência Molecular / Catálise / Sequência de Aminoácidos / Clonagem Molecular / DNA Complementar / Saussurea / Chalconas Idioma: Chinês Revista: Chinese Journal of Biotechnology Ano de publicação: 2011 Tipo de documento: Artigo