scholarly journals Purification and Properties of Rat Liver Tyrosine Aminotransferase

1969 ◽  
Vol 244 (13) ◽  
pp. 3618-3624 ◽  
Author(s):  
F A Valeriote ◽  
F Auricchio ◽  
G M Tomkins ◽  
D Riley
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Purification And Properties

scholarly journals Regulation of Tyrosine Aminotransferase in Rat Liver

1973 ◽  
Vol 248 (13) ◽  
pp. 4528-4531
Author(s):  
Ronald W. Johnson ◽  
Francis T. Kenney
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase

Purification and properties of a neutral protease from rat liver chromatin

Biochemistry ◽  
1974 ◽  
Vol 13 (25) ◽  
pp. 5128-5134 ◽  
Author(s):  
Ming Ta Chong ◽  
William T. Garrard ◽  
James Bonner
Keyword(s):  
Rat Liver ◽  
Neutral Protease ◽  
Purification And Properties ◽  
Liver Chromatin

scholarly journals The effects of salicylate on the activity of rat liver tyrosine–2-oxoglutarate aminotransferase in vitro and in vivo

1972 ◽  
Vol 126 (2) ◽  
pp. 347-350 ◽  
Author(s):  
A. A.-B. Badawy
Keyword(s):  
Rat Liver ◽  
Pyridoxal Phosphate ◽  
Actinomycin D ◽  
Sodium Salicylate ◽  
Intraperitoneal Administration ◽  
Tyrosine Aminotransferase ◽  
Major Effect ◽  
Endogenous Activity

1. Salicylate, in concentrations of 0.25mm and above, enhances the basal activity of tyrosine–2-oxoglutarate aminotransferase in homogenates of rat liver incubated in the absence of added pyridoxal 5′-phosphate (endogenous activity). The effect is decreased by increasing the concentration of the cofactor. 2. The intraperitoneal administration of sodium salicylate enhances the activity of rat liver tyrosine aminotransferase; the major effect during the first hour being on the enzyme in the absence of added pyridoxal phosphate. Actinomycin D prevents the induction of the enzyme by cortisol and tryptophan. Induction by pyridoxine or salicylate is 50% inhibited by actinomycin D. The effects of the injections of various combinations of cortisol, pyridoxine and salicylate were also studied in the absence or presence of actinomycin D. 3. It is suggested that salicylate induces rat liver tyrosine aminotransferase by displacing its protein-bound cofactor and that a cofactor-type induction of the hepatic enzyme occurs in pyridoxine-treated rats.

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.

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