Abstract
Cysteamine oxygenase has been analysed for the presence of metals, by spectrographic analysis, and X‐ray fluorescence. Iron, copper, and zinc have been found in the enzyme in the quantity accounting for 1 atom of each metal per molecule of enzyme.Passage of the enzyme through a chelating resin column did not appreciable change the specific activity but the metal content was decreased below the value of one atom per molecule of enzyme. Possible explanations for this finding are suggested.The effect of several chelating agents on enzymic activity has been studied. All the chelating agents assayed were found inhibitory when tested in suitable concentration. The highest inhibition was observed with 8‐hydroxyquinoline, diethyldithiocarbamate and o‐phenanthroline. KCN also was a good inhibitor.It is concluded that cysteamine oxygenase is a metal‐containing enzyme and that the metals should play a functional role.
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