beta-Oxidative cleavage of octanoyl- and dodecanoyl-CoA in rat liver cytoplasm.

[12-14C] Dodecanoyl-CoA and [8-14C] octanoyl-CoA were tested as substrates for shortening the chain by two carbon atoms using both the 105,000 x g soluble fraction and the sonicated mitochondrial fraction of rat liver homogenate as the enzyme source. Both substrates were metabolized by the cytoplasmic enzymes giving rise to the accumulation of intermediates of the beta-oxidation process without formation of two carbon units from the methyl carbon of the acyl residue. A new method is described which allows quantitative estimation of volatile fatty acids formed by beta-oxidation of dodecanoyl- and octanoyl- Coenzyme A.