Richard A. Jacobs

TL;DR: It is suggested that the acetyl-CoA carboxylase from the tumors is the same enzyme as that from host liver, and that the increased activity in the tumor is due to an increased amount of enzyme rather than a structurally altered enzyme.

TL;DR: Equivalence point determinations using an antibody against acetyl-CoA carboxylase indicate that the increase in enzyme activity results from increased enzyme content in the cells rather than from activation of preformed enzyme.

TL;DR: Total cellular levels of these metabolites are not directly responsible for regulation of the rate of acetate incorporation into fatty acids, suggesting that the site of action of fatty acids is intracellular.

TL;DR: Feeding a low fat, biotin-deficient diet to young rats for 1 to 2 weeks leads to a decrease in acetyl coenzyme A carboxylase levels in epididymal adipose tissue with accumulation of the apoenzyme, demonstrating the marked difference in the metabolism of the enzyme in these tissues.