Abstract
IN continuation of the studies on pyridoxamine phosphate oxidase and pyridoxal phosphatase activities by Escherichia coli1,2 and their significance in the control of amino-acid metabolism, we have now prepared both acid and alkaline phosphatases from extracts of the strains of E. coli which we are using in Leeds and examined their action on the tryptophanase system. We had previously shown that such extracts had a high acid phosphatase and low alkaline phosphatase activity, but that a mammalian acid phosphatase did not dephosphorylate pyridoxal phosphate whereas an alkaline phosphatase did2.
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