Immunoquantitation of liver glucose-6-phosphate dehydrogenase and malic enzyme in normally and prematurely weaned rats

1983 ◽  
Vol 61 (10) ◽  
pp. 1108-1113 ◽  
Author(s):  
Donald W. Back ◽  
Joseph F. Angel

Rat liver glucose-6-phosphate dehydrogenase and malic enzyme were purified and rabbit serum antibodies were prepared against each enzyme. The activities and quantities of both enzymes in the livers of infant rats were subsequently determined during the weaning period. Glucose-6-phosphate dehydrogenase was present and active in the liver of spontaneously weaned rats on postnatal day 17 and increased from postnatal day 21 onwards. Malic enzyme and its activity were undetectable on postnatal day 17. The latter enzyme was detected on postnatal day 21 and increased rapidly afterwards. These changes occurred sooner and were more pronounced when the rats were weaned prematurely on postnatal day 17, especially when the diet contained sucrose. The activities of both enzymes were highly correlated with the amounts of enzyme protein present throughout the experiment. It appeared that the activities of both enzymes in infant rats were likely to be regulated by altering their synthesis and (or) degradation, rather than by activation of existing proteins, assuming that the latter can be detected by the antibodies employed.

1988 ◽  
Vol 16 (1) ◽  
pp. 33-34
Author(s):  
PARMJIT S. SOHAL ◽  
WILLIAM J. ROESLER ◽  
RAMJI L. KHANDELWAL ◽  
JOSEPH F. ANGEL

1997 ◽  
Vol 75 (4) ◽  
pp. 487-492 ◽  
Author(s):  
N Sanz ◽  
C Díez-Fernández ◽  
AM Valverde ◽  
M Lorenzo ◽  
M Benito ◽  
...  

1981 ◽  
Vol 194 (1) ◽  
pp. 249-255 ◽  
Author(s):  
B Mittal ◽  
C K R Kurup

Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine O-acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in hepatic mitochondria shows a time lag during which the activity increases in the microsomal and peroxisomal fractions. The enzyme induced in the particulate fractions is identical with one normally present in mitochondria. The increase in enzyme activity is prevented by inhibitors of RNA and general protein synthesis. Mitochondrial protein-synthetic machinery does not appear to be involved in the process. Immunoprecipitation shows increased concentration of the enzyme protein in hepatic mitochondria isolated from drug-treated animals. In these animals, the rate of synthesis of the enzyme is increased 7-fold.


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