2,4-Dichlorophenoxyacetic Acid Inhibition of Castor Bean Lipase

Abstract

The activity of castor bean lipase was inhibited by 10% by a 3.03 x 10-4 [image] concn. of the monohydrate of Na 2,4-dichlorophenoxyacetate, and 70% by a 3 x 10-1 [image] concn. as measured by the rate of liberation of free acid from olive oil. The butyl ester of the 2,4-D acid as such did not inhibit the activity of the enzyme, but was hydrolyzed by the enzyme, and the liberated acid was an active enzyme inhibitor; thus inhibition by the ester required a much longer time to reach a maximum than did inhibition by the salt.