Abstract
The conversion of kynurenine into kynurenic acid and anthranilic acid in both normal and Schistosoma mansoni-infested mouse liver was investigated. It was found that in the S. mansoni-infested mouse liver there is probably a deficiency of pyridoxal phosphate that resulted in an inhibition of kynurenine transaminase and a low production of kynurenic acid. Deoxypyridoxine and its phosphorylated derivative inhibited kynurenine transaminase in the normal liver in a pattern qualitatively similar to that observed with infested liver. The lowered concentration of pyridoxal phosphate in the infested liver is discussed in view of the possibility of two combined mechanisms: (a) an antimetabolite being secreted by the infesting worms or present in its eggs that partially inhibited the phosphorylation of pyridoxal, and (b) concentration of pyridoxal phosphate by the worms, resulting in a lowered concentration of the cofactor in the host tissue.
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