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A technical note on esterase D subtyping

The electrophoretic behavior of esterase D (E.C. 3.1.1.1.) allozymes 1, 2 and 5 was studied in various buffers and pH ranges, and compared with results obtained on isoelectric focusing. It is shown that the relative mobility of ESD 2 and 5 allozymes is reversed according to the pH of the buffer system. In acidic pH ranges the mobility is: cathode 1<2<5 anode; using the same buffer system in basic pH ranges the following order is observed: 1<5<2. Technical improvements in agarose gel electrophoresis leading to a considerable economical advantage over the previously described methods are presented.