Abstract
The specificity of the lead method for phosphorylase was investigated in rat liver by gel electrophoresis and biochemical and histochemical assays in comparison with the iodine method.It was found that in the case of the iodine method, inhibition of amylase by ethylenediamine tetraacetate was necessary for a full demonstration of the phosphorylase activity, while in the lead method such interference of the phosphorylase staining by amylase was not a serious problem.Phosphorylase was markedly inhibited by lead ions and glutaraldehyde, but quantitative and histochemical data indicated that glycogen synthesis could occur even in the presence of lead ions in frozen-substituted sections before and after fixation in glutaraldehyde.
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