Acetate binding of spinach chloroplasts as a facet of fatty acid synthesis.

A particulate fraction of spinach chloroplasts is the major site of binding when either acetate or acetyl-CoA is used as substrate. The acetate is linked covalently, and the binding is inhibited by reagents which react with sulfhydryl groups. The amount of acetate bound is lowered by both citrate and oxaloacetate; however, the binding is not reversed by oxaloacetate. Reversal of binding is also not brought about by the addition of unlabeled acetyl-CoA. If cofactors for fatty acid synthesis and cold acetyl-CoA are added, the binding of labeled acetate is reversed. Acyl carrier protein from E. coli increases the binding of labeled acetate.