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The Interaction of Dithiothreitol and Acetyl Coenzyme A in a Radiochemical Assay for Rat Brain ATP:Citrate Oxaloacetate Lyase

Abstract: [14C]Acetyl‐CoA was found to react spontaneously with dithiothreitol to give a relatively apolar product which was readily extractable into a butanol‐toluene scintillant. This technique was used in a rapid, reproducible assay for rat brain ATP:citrate lyase using [1,5‐14C]citrate as substrate. The tissue extract, a 14,000 g supernatant, exhibited a lyase activity of approximately 7 nmol acetyl‐CoA produced/min per mg supernatant protein, and was inhibited ≥79% by α‐ketoglutaric acid (10 mm), Cu2+ (1 mm)and Zn2+(1 mm). [14C]Oxaloacetate, [14C]malate and endogenous citrate synthase were found not to interfere significantly with lyase estimations, but NADH was required in the reaction mixture to inhibit acetyl‐CoA hydrolase activity.