Abstract
1. 1. An enzyme that catalyses the cleavage of lanthionine to cysteine, ammonia and pyruvate was purified 100-fold from the larval fat body of the silkworm, Bombyx mori. 2. 2. The mol. wt of the enzyme is 200,000, the isoelectric point is pH 5.5, the pH optimum is 8.0, the K m value for dl( meso)-lanthionine is 3.8 x 10 −3 M and pyridoxal phosphate is a necessary cofactor. 3. 3. The purified enzyme exhibited cystathionase activity and the ratio of the enzyme to cystathionase was almost constant during the purification. The enzyme activity was inhibited by the addition of cystathionine. The present results suggest that the enzyme is identical with cystathionase.
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