The Enzymic Degradation of Hematin Compounds I

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Abstract
1) An enzyme which converts hemin to verdohemochrome was isolated as an active cell-free preparation from bovine liver. A partial purification was made by fractionating a buffer extract of acetone-dried powder of bovine liver with ammonium sulfate. The most active enzyme protein was precipitated between 0.33 and 0.66 saturation. 2) This enzyme protein requires a co-enzyme for its activity. 3) The optimum pH for the enzyme activity lies on pH about 8.6. 4) This enzyme is completely inactivated by treating it at 80° for 5 minutes. 5) The effects of concentrations of enzyme and substrate on the reaction rate were also studied.

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