Purification and activity evaluation of methionine synthase / 药学学报
Acta Pharmaceutica Sinica
;
(12): 1463-1469, 2012.
Artículo
en Chino
| 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:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Farmacología
/
Quinazolinas
/
5-Metiltetrahidrofolato-Homocisteína S-Metiltransferasa
/
Tiofenos
/
Química
/
Tetrahidrofolatos
/
Metotrexato
/
Ratas Wistar
/
Electroforesis en Gel de Poliacrilamida
/
Antagonistas del Ácido Fólico
Tipo de estudio:
Estudio pronóstico
Límite:
Animales
Idioma:
Chino
Revista:
Acta Pharmaceutica Sinica
Año:
2012
Tipo del documento:
Artículo
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