Action of the phosphonic analogue of tyrosine and of other tyrosine derivatives on rat liver tyrosine aminotransferase

Amino Acids ◽  
1993 ◽  
Vol 5 (1) ◽  
pp. 33-37 ◽  
Author(s):  
A. Iron ◽  
E. Neuzil ◽  
A. Cassaigne
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Tyrosine Derivatives ◽  
Phosphonic Analogue ◽  
Phosphonic Analogue Of Tyrosine

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

scholarly journals Evidence for a dual effect of dibutyryl cyclic AMP on the synthesis of tyrosine aminotransferase in rat liver.

1982 ◽  
Vol 257 (5) ◽  
pp. 2386-2390 ◽  
Author(s):  
T Noguchi ◽  
M Diesterhaft ◽  
D Granner
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Dibutyryl Cyclic Amp ◽  
Dual Effect

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.

scholarly journals Purification and characterization of rat liver tyrosine aminotransferase

FEBS Letters ◽  
1977 ◽  
Vol 75 (1-2) ◽  
pp. 221-225 ◽  
Author(s):  
A. Belarbi ◽  
C. Bollack ◽  
N. Befort ◽  
J.P. Beck ◽  
G. Beck
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Purification And Characterization

Studies on the conversion of multiple forms of tyrosine aminotransferase in rat liver

1976 ◽  
Vol 177 (1) ◽  
pp. 185-195 ◽  
Author(s):  
Jesus M. Rodriguez ◽  
Henry C. Pitot
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Multiple Forms

scholarly journals Inactivation of tyrosine aminotransferase in neutral homogenates and rat liver slices

1972 ◽  
Vol 129 (5) ◽  
pp. 1131-1138 ◽  
Author(s):  
F. Auricchio ◽  
L. Mollica ◽  
A. Liguori
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Acid Concentration ◽  
Tyrosine Aminotransferase ◽  
Amino Acid Concentration ◽  
Acidic Ph ◽  
Ph Values ◽  
Neutral Ph ◽  
Liver Slices

Inactivation of tyrosine aminotransferase induced in vivo by triamcinolone was studied in a homogenate incubated at neutral pH values. The integrity and the presence of subcellular particles together with a compartment of acidic pH are necessary for inactivation of tyrosine aminotransferase. It is suggested that tyrosine aminotransferase is inactivated inside lysosomes. The system responsible for inactivation of tyrosine aminotransferase was partially purified and identified with lysosomal cathepsins B and B1. Inactivation of tyrosine aminotransferase in liver slices is controlled by the amino acid concentration and strongly stimulated by cysteine. 3,3′,5-Tri-iodo-l-thyronine reversibly and strongly decreases the rate of inactivation of tyrosine aminotransferase. The effect is not due to an increased rate of tyrosine aminotransferase synthesis.

Induction of Tyrosine Aminotransferase and Depression of Protein Synthesis in Rat Liver by a Tryptophan-free Mixture of Amino Acids

1974 ◽  
Vol 104 (9) ◽  
pp. 1149-1156 ◽  
Author(s):  
Brigitte Pamart ◽  
Anik Girard-Globa ◽  
Geneviève Bourdel
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Rat Liver ◽  
Tyrosine Aminotransferase
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