Phosphoenolpyruvate carboxykinase (guanosine triphosphate) from rat liver cytosol. Separation of homogeneous forms of the enzyme with high and low activity by chromatography on agarose-hexane-guanosine triphosphate

Biochemistry ◽  
1978 ◽  
Vol 17 (25) ◽  
pp. 5321-5329 ◽  
Author(s):  
Giovanna Colombo ◽  
Gerald M. Carlson ◽  
Henry A. Lardy
Keyword(s):  
Rat Liver ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Guanosine Triphosphate ◽  
Liver Cytosol ◽  
Low Activity ◽  
Rat Liver Cytosol

scholarly journals Alterations in translatable messenger RNA coding for phosphoenolpyruvate carboxykinase (GTP) in rat liver cytosol during deinduction.

1978 ◽  
Vol 253 (12) ◽  
pp. 4327-4332
Author(s):  
D. Kioussis ◽  
L. Reshef ◽  
H. Cohen ◽  
S.M. Tilghman ◽  
P.B. Iynedjian ◽  
...  
Keyword(s):  
Rat Liver ◽  
Messenger Rna ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Activation and inactivation of phosphoenolpyruvate carboxykinase by ferrous ions

1980 ◽  
Vol 185 (2) ◽  
pp. 451-454 ◽  
Author(s):  
C H Reynolds
Keyword(s):  
Rat Liver ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Protein Fractions ◽  
Time Dependent ◽  
Ferrous Ions ◽  
Irreversible Loss ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Phosphoenolpyruvate carboxykinase from rat liver cytosol is activated by Fe2+ ions in either direction of catalysis. Preincubation of the purified enzyme with Fe2+ ions causes a time-dependent irreversible loss of activity; this is not seen with unpurified enzyme. Purified enzyme can be protected from inactivation by Fe2+ ions by partially purified protein fractions from liver (ferroactivator fractions). The possible role of ferroactivator and Fe2+ ions in regulating phosphoenolpyruvate carboxykinase is discussed.

scholarly journals Synthesis of phosphoenolpyruvate from propionate in sheep liver

1971 ◽  
Vol 124 (5) ◽  
pp. 867-876 ◽  
Author(s):  
R. M. Smith ◽  
W. S. Osborne-White
Keyword(s):  
Rat Liver ◽  
Malic Enzyme ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Liver Cytosol ◽  
Sheep Liver ◽  
Mitochondrial Aconitase ◽  
Low Activity ◽  
Very High

1. Utilization of propionate by sheep liver mitochondria was stimulated equally by pyruvate or α-oxoglutarate, with formation predominantly of malate. Pyruvate increased conversion of propionate carbon into citrate, whereas α-oxoglutarate increased formation of phosphoenolpyruvate. The fraction of metabolized propionate converted into phosphoenolpyruvate was about 17% in the presence or absence of α-oxoglutarate and about 7% in the presence of pyruvate. Pyruvate consumption was inhibited by 80% by 5mm-propionate. 2. Compared with rat liver, sheep liver was characterized by very high activities of phosphoenolpyruvate carboxykinase and moderately high activities of aconitase in the mitochondria and by low activities of ‘malic’ enzyme, pyruvate kinase and lactate dehydrogenase in the cytosol. Activities of phosphoenolpyruvate carboxy-kinase were similar in liver cytosol from rats and sheep. Activities of malate dehydrogenase and NADP-linked isocitrate dehydrogenase in sheep liver were about half those in rat liver. 3. The phosphate–dicarboxylate antiport was active in sheep liver mitochondria, but compared with rat liver mitochondria the citrate–malate antiport showed only low activity and mitochondrial aconitase was relatively inaccessible to external citrate. The rate of swelling of mitochondria induced by phosphate in solutions of ammonium malate was inversely related to the concentration of malate. 4. The results are discussed in relation to gluconeogenesis from propionate in sheep liver. It is proposed that propionate is converted into malate by the mitochondria and the malate is converted into phosphoenolpyruvate by enzymes in the cytosol. In this way sufficient NADH would be generated in the cytosol to convert the phosphoenolpyruvate into glucose.

scholarly journals Transformation of the glucocorticoid receptor in rat liver cytosol by lysosomal enzymes.

1979 ◽  
Vol 254 (5) ◽  
pp. 1537-1539 ◽  
Author(s):  
J. Carlstedt-Duke ◽  
O. Wrange ◽  
E. Dahlberg ◽  
J.A. Gustafsson ◽  
B. Högberg
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Development of an [3H] glucocorticoid exchange assay in rat liver cytosol

Steroids ◽  
1981 ◽  
Vol 37 (4) ◽  
pp. 409-421 ◽  
Author(s):  
Ashutosh Banerji ◽  
Mohammed Kalimi
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Rat Liver Cytosol
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