Abstract
EARLIER investigations1,2 of peroxidase activity in homogenates of rat kidney and liver have led to the conclusion that the total activity of the soluble fraction can be accounted for by its hæmoglobin content. Several objections can, however, be raised against this. As hæmoglobin (as well as its derivatives) and catalase are the two main complicating factors in the determination of endogenous peroxidase activity of tissue homogenates, the ideal estimation procedure is that which completely removes the hæmoglobin and the catalase from the homogenates. Complete removal of hæmoglobin is impossible. However, a method is described here for preparing a tissue homogenate free from catalase and containing only minimal amounts of hæmoglobin.
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FLATMARK, T. Demonstration of Peroxidase Activity in the Rat Kidney and Liver: Peroxidase Effect of Cytochrome c. Nature 196, 894–895 (1962). https://doi.org/10.1038/196894a0
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DOI: https://doi.org/10.1038/196894a0
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