Purification and activity evaluation of methionine synthase / 药学学报
Acta Pharmaceutica Sinica
;
(12): 1463-1469, 2012.
Artigo
em Chinês
| WPRIM
| ID: wpr-274637
ABSTRACT
Methionine synthase (MS, EC2.1.1.13), a key enzyme in the folate metabolism area catalyzing methyl transfer from N5-methyltetrahydrofolate to homocysteine to give tetrahydrofolate and methionine, takes a core position in folate cycle, one-carbon-unit transfer and sculpture amino acid pathways. Cobalamin-dependent methionine synthase was purified from rat liver. The enzyme was purified 609-fold to near homogeneity by batch chromatography on DE-52, anion-exchange chromatography on Q Sepharose Fast Flow and CHT-I hydroxyapatite column and was identified by SDS-PAGE and Western blotting. The enzyme activity was determined by spectrophotometric assay. In addition, the influencing factor and optimal reaction condition were performed. The steady state kinetic of rat liver methionine synthase was similar to that of other mammalian cobalamin-dependent methionine synthase which employed a Ping-Pong mechanism. The result indicated that cobalamin-dependent methionine synthase purified from rat liver is suitable for screening and studying methionine synthase specific inhibitors.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Farmacologia
/
Quinazolinas
/
5-Metiltetra-Hidrofolato-Homocisteína S-Metiltransferase
/
Tiofenos
/
Química
/
Tetra-Hidrofolatos
/
Metotrexato
/
Ratos Wistar
/
Eletroforese em Gel de Poliacrilamida
/
Antagonistas do Ácido Fólico
Tipo de estudo:
Estudo prognóstico
Limite:
Animais
Idioma:
Chinês
Revista:
Acta Pharmaceutica Sinica
Ano de publicação:
2012
Tipo de documento:
Artigo
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