Abstract
A procedure for assaying leukotriene C 4 synthase activity in cell-free extracts has been presented. Leukotriene A 4 methyl ester was as active a substrate as leukotriene A 4 (Na salt) for the synthesis. The methyl ester is the substrate of choice, because (1) it is more stable than the sodium salt, (2) it is not a substrate of epoxide hydrolase for leukotriene B 4 synthesis, and (3) it gives a lower blank than an equimolar concentration of leukotriene A 4. The enzyme activity in rat liver, guinea pig and human lungs, and human nasal polyp was chiefly membrane-bound, although the cytosol contained some activity.
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