scholarly journals Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria

1976 ◽  
Vol 159 (3) ◽  
pp. 683-687 ◽  
Author(s):  
M Grunwald ◽  
H Z Hill
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Kinetic Behaviour ◽  
Two Peaks ◽  
Glucose 6 Phosphate Dehydrogenase

Glucose 6-phosphate dehydrogenase activity in rat liver mitochondria can be released by detergent. The released activity is separated by chromatography into two peaks. One peak has the kinetic behaviour and mobility similar to the soluble sex-linked enzyme, whereas the other peak is similar to the microsomal hexose 6-phosphate dehydrogenase. There is no evidence for the existence of a new glucose 6-phosphate dehydrogenase activity in rat liver mitochondria.

scholarly journals Characterization of a DNA primase from rat liver mitochondria.

1986 ◽  
Vol 261 (14) ◽  
pp. 6571-6577
Author(s):  
B J Ledwith ◽  
S Manam ◽  
G C Van Tuyle
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Dna Primase

Characterization of betaine efflux from rat liver mitochondria

1993 ◽  
Vol 1141 (2-3) ◽  
pp. 269-274 ◽  
Author(s):  
Richard K. Porter ◽  
John M. Scott ◽  
Martin D. Brand
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

scholarly journals Inhibition of carbon dioxide fixation by lead acetate in rat liver mitochondria

1977 ◽  
Vol 166 (1) ◽  
pp. 75-79 ◽  
Author(s):  
J M Amatruda ◽  
A J Staton ◽  
L A Kiesow
Keyword(s):  
Rat Liver ◽  
Lead Acetate ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Co2 Fixation ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Lead Salts ◽  
Lactate And Pyruvate ◽  
Gluconeogenesis From Alanine ◽  
Glucose 6 Phosphate Dehydrogenase

These studies were undertaken to determine the mechanism by which intravenously administered lead salts inhibit hepatic gluconeogenesis. Within 1 h after the intravenous administration of lead acetate (10 mg), there is 97% inhibition of CO2 fixation in isolated rat liver mitochondria. This effect is concentration-dependent. The induction of phosphoenolpyruvate carboxykinase activity observed with starvation was also inhibited by intravenously administered lead acetate, but the activities of pyruvate kinase, glucose 6-phosphate dehydrogenase and pyruvate carboxylase were unaffected, as was the oxidation of palmitate and palmitoyl-CoA by mitochondria from Pb2+-treated animals. The addition of reduced glutathione to mitochondria from Pb2+-treated animals had no effect on the inhibited CO2 fixation. ATP concentrations in mitochondria from Pb2+-treated animals are decreased and the dose-response relationships for the effect of Pb2+ on CO2 fixation and ATP concentrations correspond. We conclude that the decrease in mitochondrial ATP in Pb2+-treated animals is probably responsible for the marked inhibition ov CO2 fixation, and hence the impairment of gluconeogenesis from alanine, lactate and pyruvate observed by others.

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