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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.


Subject(s)
Binding Sites , Diethyl Pyrocarbonate , Histidine/physiology , Indicators and Reagents , Leucine Transaminase , Plants/enzymology , Rose Bengal , Transaminases/antagonists & inhibitors
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