Abstract
Summary
The existence of PAPS-transferase in chick liver was demonstrated and this enzyme was isolated and partially purified. The requirement of PAPS as a substrate for this transferase in the synthesis of taurine was demonstrated. Studies on the origin of the acceptor molecule and the carbon moiety which ultimately becomes taurine indicated that methionine may be directly involved in this synthesis. Studies showed that neither the carboxyl nor the methyl carbon of methionine became taurine carbon, while some of the remaining carbons of methionine appeared in the taurine molecule.
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