Abstract
A method is described for partially purifyingDrosophila tryptophan pyrrolase. The enzyme, which appears to have a heme prosthetic group, is sensitive to dialysis, but the addition of hematin does not restore any of the lost activity. The enzyme requires activation and 2-mercaptoethanol is much preferred to ascorbate as the activator because in the presence of ascorbate a non-enzymatic reaction interferes. Serological cross reaction between antibodies toPseudomonas tryptophan pyrrolase and theDrosophila enzyme does not occur. By several criteria, the enzyme from suppressed-vermilion flies is indistinguishable from the wild-type enzyme.
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