Abstract
1. 1. Citrate synthase was isolated from the fast adductor muscle of the scallop Pecten alba. The enzyme has a molecular weight of about 90,000 as estimated by gel filtration, and resembles other “small” citrate synthases in its relative insensitivity to inhibition by NADH ( K i 1.6 mM). 2. 2. ATP, ADP, AMP and NADH are competitive inhibitors with respect to acetyl CoA, citrate is competitive with respect to oxaloacetate, while ketoglutarate displays mixed inhibition with respect to oxaloacetate. During the aerobic-anaerobic transitions that occur in the scallop fast adductor muscle, citrate synthase activity may be regulated by the availability of oxaloacetate and acetyl CoA, and by the influence of competitive inhibitors on the affinity of the enzyme for these substrates.
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