Abstract
Rat liver acetyl-CoA carboxylase was purified by affinity chromatography. An affinity adsorbent was prepared by coupling an inhibitor of liver acetyl-CoA carboxylase, kynurenate, to aminoethyl agarose synthesized from ethylene diamine and CNBr-activated agarose. On chromatography of the ammonium sulfate fraction of rat liver soluble supernatant on a kynurenate-agarose column in the presence of citrate, acetyl-CoA carboxylase was purified about 40 fold with a yield of 90%.
