Your browser doesn't support javascript.
loading
Purification and characterization of dihydrofolate reductase of Plasmodium falciparum expressed by a synthetic gene in Escherichia coli.
Sano, G; Morimatsu, K; Horii, T.
Afiliação
  • Sano G; Department of Protozoology and Parasitology, Osaka University, Japan.
Mol Biochem Parasitol ; 63(2): 265-73, 1994 Feb.
Article em En | MEDLINE | ID: mdl-8008023
We have expressed the dihydrofolate reductase (DHFR) part of the DHFR-thymidylate synthetase complex of P. falciparum in Escherichia coli, by constructing a gene with synthetic oligonucleotides that changed the gene's codon usages. The induced expression in an E. coli cell of the synthetic gene yielded a product that constituted about 30% of the total bacterial protein. The product was precipitated in an inclusion body in a cell. Its enzymatic activity was restored after denaturation and renaturation procedures with guanidine-HCl. Recombinant DHFRs with Ser or Thr at position 108 were prepared. Kinetic characterization showed that the DHFRSer108 has less of an affinity for NADPH and dihydrofolate than the DHFRThr108.
Assuntos
Buscar no Google
Coleções: 01-internacional Contexto em Saúde: 2_ODS3 / 3_ND Base de dados: MEDLINE Assunto principal: Plasmodium falciparum / Tetra-Hidrofolato Desidrogenase / Genes de Protozoários / Genes Sintéticos Limite: Animals Idioma: En Revista: Mol Biochem Parasitol Ano de publicação: 1994 Tipo de documento: Article
Buscar no Google
Coleções: 01-internacional Contexto em Saúde: 2_ODS3 / 3_ND Base de dados: MEDLINE Assunto principal: Plasmodium falciparum / Tetra-Hidrofolato Desidrogenase / Genes de Protozoários / Genes Sintéticos Limite: Animals Idioma: En Revista: Mol Biochem Parasitol Ano de publicação: 1994 Tipo de documento: Article