scholarly journals Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: Recurrence of tyrosine aminotransferase activity in the Iα subfamily

2013 ◽  
Vol 81 (9) ◽  
pp. 1593-1609 ◽  
Author(s):  
Kathryn E. Muratore ◽  
Barbara E. Engelhardt ◽  
John R. Srouji ◽  
Michael I. Jordan ◽  
Steven E. Brenner ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Tyrosine Aminotransferase ◽  
Function Prediction ◽  
Molecular Function ◽  
Aminotransferase Activity

scholarly journals Biphasic effect of acute ethanol administration on rat liver tyrosine-2-oxoglutarate aminotransferase activity

1980 ◽  
Vol 186 (3) ◽  
pp. 755-761 ◽  
Author(s):  
A A B Badawy ◽  
B M Snape ◽  
M Evans
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Actinomycin D ◽  
Tyrosine Aminotransferase ◽  
Ethanol Metabolism ◽  
Ethanol Administration ◽  
Aminotransferase Activity ◽  
Biphasic Effect ◽  
Initial Decrease ◽  
Acute Ethanol

1. Acute ethanol administration causes a biphasic change in rat liver tyrosine aminotransferase activity. 2. The initial decrease is significant with a 200 mg/kg dose of ethanol, is prevented by adrenoceptor-blocking agnets and by reserpine, but not by inhibitors of ethanol metabolism, and exhibits many of the characteristics of the inhibition caused by noradrenaline. 3. The subsequent enhancement of the enzyme activity by ethanol is not associated with stabilization of the enzyme, but is sensitive to actinomycin D and cycloheximide. 4. It is suggested that the initial decrease in aminotransferase activity is caused by the release of catecholamines, whereas the subsequent enhancement may be related to the release of glucocorticoids.

Tyrosine aminotransferase activity in the benzene intoxicated rat

1985 ◽  
Vol 34 (1) ◽  
pp. 36-44
Author(s):  
M. Bong ◽  
A. Michalska ◽  
T. Laskowska-Klita ◽  
T. Szymczyk
Keyword(s):  
Tyrosine Aminotransferase ◽  
Aminotransferase Activity
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