Transformation of Leukotriene D₄ Catalyzed by Lysosomal Cathepsin H of Rat Liver

抄録

Among several intracellular protease tested, cathepsin H transformed leukotriene D₄ to E₄ with a release of glycine in a stoichiometric quantity. Under the optimal conditions the rate of leukotriene D₄ transformation by cathepsin H was about 3% of the hydrolysis rate of α-N-benzoyl-DL-arginine-2-naphthylamide which is commonly utilized as a very efficient substrate to test the peptidase activity of the enzyme. Leukotriene C₄ was not transformed to leukotriene D₄, by cathepsin H. Neither cathepsin B nor C was active with leukotrienes C₄ and D₄.