Abstract
1. 1. Partially purified acetyl-CoA carboxylase (acetyl-CoA:CO 2 ligase (ADP), EC 6.4.1.2) from the livers of rats starved for 12 h is activated by incubation at 37° for 3–4 h; in contrast to previous reports the presence of citrate is not required for activation. The rate of [ 14C]acetyl-CoA incorporation into fatty acids by 100 000 × g supernatant preparations form rat liver is also increased by incubation without citrate. 2. 2. Acetyl CoA carboxylase activities of partially purified and 100 00 × g supernatant preparations activated by treatment with trypsin were found in the low-density portions of sucrose gradients in contrast to preparations activated by incubation with citrate .
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