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
Article
in English
| 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Plants
/
Rose Bengal
/
Binding Sites
/
Diethyl Pyrocarbonate
/
Leucine Transaminase
/
Transaminases
/
Histidine
/
Indicators and Reagents
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1989
Type:
Article
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