Enzymatic activities of cytoplasmic and of microsomal acetyl-CoA carboxylase of rat epididymal adipose tissue; different regulatory effects of a short-term fasting and palmitoyl-CoA on these two enzymes.
The existence of a microsomal acetyl-CoA carboxylase in the rat epididymal adipose tissue was demonstrated in vitro in the present study. Its specific activity was of the same order of magnitude as that of the cytoplasmic acetyl-CoA carboxylase. The effect of several experimental conditions on the enzymatic activities of both enzymes were tested; fasting for 24 hr strongly increased (2.5-4 times) the activity of the microsomal enzyme while the cytoplasmic enzyme remained unchanged. Palmitoyl-CoA (1 and 5 microM), an inhibitor of acetyl-CoA carboxylase, had a greater effect on the cytoplasmic (33 and 88% inhibition) than on the microsomal enzyme (0 and 37% inhibition).
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D003593:Cytoplasm / Q000201:enzymology*; D004822:Epididymis / Q000201:enzymology; D005215:Fasting; D008025:Ligases / Q000378:metabolism*; D008297:Male; D008861:Microsomes / Q000201:enzymology*; D010171:Palmitoyl Coenzyme A / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013997:Time Factors
D000214:Acyl Coenzyme A; D010171:Palmitoyl Coenzyme A; D008025:Ligases; D000103:Acetyl-CoA Carboxylase