Inactivation of leucine aminotransferase with diethylpyrocarbonate and rose bengal: evidence for an active site histidine residue.
Indian J Biochem Biophys
;
1989 Jun; 26(3): 136-9
Artigo
em Inglês
| IMSEAR
| ID: sea-28155
ABSTRACT
Modification of leucine aminotransferase by diethylpyrocarbonate or rose bengal-sensitized photo-oxidation caused rapid inactivation of the enzyme. The inactivation of leucine aminotransferase depended on the concentration of the reagent, the time of incubation and exhibited pseudo-first order kinetics. Rose bengal-sensitized photo-oxidation was maximum at pH 6.5 and 9. Substrates leucine and alpha-ketoglutarate protected the enzyme against inactivation by these reagents, thus suggesting participation of histidine residue at the substrate binding site.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Plantas
/
Rosa Bengala
/
Sítios de Ligação
/
Dietil Pirocarbonato
/
Leucina Transaminase
/
Transaminases
/
Histidina
/
Indicadores e Reagentes
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1989
Tipo de documento:
Artigo
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