Peroxidase isoenzymes may be separated on acrylamide gels and then detected by supplying the substrate in an appropriate reaction system. One such system frequently used contains guaiacol as the hydrogen donor, although this compound has certain drawbacks. Ways of circumventing these drawbacks are suggested, so that quantitative estimates of the activity of individual peroxidase isoenzymes may be obtained.
Isoenzymes of peroxidase were separated on acrylamide gels in 2 genotypes of Linum usitatissimum L. and their F 1, F 2 and first backcross progeny. Active extracts were obtained from homogenates of main stem tissue; activity was measured both before and after electrophoretic separation. The relationship of isoenzyme activity to gross (prior to electrophoretic separation) activity was investigated, as well as the relative behaviour of isoenzyme activity in the various genotypes and generations. Gross activity was correlated with isoenzyme activity; there was also evidence of maternal as well as genetic effects on isoenzyme activity.
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