Abstract
CATALASE, a hæmoprotein normally present in erythrocytes, can be separated from hæmoglobin by electrophoresis of hæmolysates on starch gel. The production of gas bubbles with hydrogen peroxide, and enzyme assays of eluates from segments of the gel, have shown that, after electrophoresis, erythrocytic catalase is confined to one discrete zone1. This zone stained weakly with naphthalene black, but, with benzidine or o-tolidine, showed a strong colour reaction, similar to the colour produced in the hæmoglobin zones. Owen, Silberman and Got2 found that o-dianisidine was the most satisfactory reagent for the detection of haemoglobin and of hæmoglobin-haptoglobin complexes on starch gel, The use of o-dianisidine as a stain for catalase on starch gel has been investigated, and it has been found that, under certain conditions, a differential colour staining can be obtained, catalase being green and hæmoglobin brown.
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References
Haut, A., Tudhope, G. R., Cartwright, G. E., and Wintrobe, M. M., J. Clin. Invest., 41, 579 (1962).
Owen, J. A., Silberman, H. J., and Got, C., Nature, 182, 1373 (1958).
Smithies, O., Biochem. J., 71, 585 (1959).
Thorup, O. A., Strole, W. B., and Leavell, B. S., J. Lab. clin. Med., 58, 122 (1961).
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TUDHOPE, G. Detection of Catalase after Electrophoresis of Hæmolysates on Starch Gel. Nature 205, 404–405 (1965). https://doi.org/10.1038/205404a0
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DOI: https://doi.org/10.1038/205404a0
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