Inhibition of rat liver acetyl CoA carboxylase by chloride.

The activity of acetyl CoA carboxylase in both crude and purified rat liver preparations was reduced in the presence of sodium or potassium chloride and increased in the presence of potassium acetate. The chloride inhibition was not competitive with bicarbonate. The use of Trischloride buffer did not alter the apparent pH optimum of the enzyme when compared with Tris-acetate buffer.