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Separation of Substrate-specific Brain Esterases by Starch-gel Electrophoresis

Naturevolume 193pages778779 (1962) | Download Citation



ZONE electrophoresis in a starch column has been found valuable for fractionation of proteins1 and enzymes2. Hunter and Burstone3 recently studied the substrate specificity of esterases of the mouse liver by starch electrophoresis, using thirty different substrates. They came to the conclusion that although substrate-dependent differences were found in the intensity of the reaction in the different bands obtained, the band patterns were essentially similar, and the differences were apparently due to differing reaction-rates on the part of the enzymes in the column rather than to all-or-none substrate specificity. In the kidney, one apparently substrate-specific band was found. The present communication aims at demonstrating that esterases of the brain, which have not previously been examined with this technique, can be resolved into separate bands which possess different substrate characteristics.


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    Hunter, R. L., and Markert, C. L., Science, 125, 1294 (1957). Markert, C. L., and Hunter, R. L., J. Histochem. Cytochem., 7, 42 (1959).

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    Hunter, R. L., and Burstone, M. S., J. Histochem. Cytochem., 8, 58 (1960).

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    Pearse, A. G. E., Histochemistry, Theoretical and Applied (Churchill, London, 1960).

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    Master, R. W. P., Biochim. Biophys. Acta, 39, 159 (1960).

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  1. Department of Anatomy, University of Helsinki, Siltavuorenpenger, Helsinki, Finland



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