Studies on ATP Citrate Lyase of Rat Liver

Publisher Website
Google Scholar
Abstract
An anti-enzyme against ATP citrate lyase [EC 4.1.3.8; ATP: citrate oxaloacetate-lyase (CoA-acetylating and ATP-dephosphorylating)] from rat liver was prepared in rabbits and the interaction of the enzyme and anti-enzyme was investigated. The reaction was complete within 10 minutes at 37°C or 1 hour at 0°C on mixing the enzyme and its anti-enzyme. At this point, over 90% of the original enzyme activity was lost with a concomitant formation of a visible precipitate. Increased enzyme activity after dietary induction is associated with an equivalent increase in the amount of protein which is immunologically indistinguishable from normal enzyme. On the contrary, decreased enzyme activity during fasting is accompanied by a comparable loss of immunologically reactive protein. The enzymes from various rat tissues, such as kidney, heart, brain and adipose tissue, cannot be distinguished from rat liver enzyme on the basis of their reactivity with rat liver anti-enzyme, while the enzymes from the livers of chick, dog, rabbit and guinea pig only react partially with the same anti-enzyme. The activities of ATP citrate lyase and fatty acid synthetase in rat liver are found to be on two immunologically distinct proteins.