|
type |
Journal Article |
authors |
Pathre, U.; Singh, A. K.; Sane, P. V. |
title |
Inactivation of leucine aminotransferase with diethylpyrocarbonate and rose bengal: evidence for an active site histidine residue |
journal |
Indian J Biochem Biophys |
Activity |
2.6.1.6 |
ui |
90152711 |
year |
(1989) |
volume |
26 |
number |
3 |
pages |
136-9. |
| |
keywords |
Binding Sites |
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. |
last changed |
2002/11/12 16:17 |
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