Abstract
Abstract It was found that 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine could act as a cofactor required by tryptophan hydroxylase partially purified from a microsome-free, final supernatant fraction of neoplastic murine mast cells. The enzyme preparation obtained was free from 5-hydroxytryptophan decarboxylase and phenylalanine hydroxylase. Kinetic studies and pH optima established differences between the mast cell enzyme and that from rat liver.
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