Abstract
Fructose diphosphate ldolases in crude muscle extracts of larval and adult Phormia regina are indistinguishable by polyacrylamide gel electrophoresis (PAGE) in several buffer systems. By contrast, larval and adult fat body aldolases differ in electrophoretic mobility, a difference shown to be due to the inequality of their net charge. Phormia regina larval muscle and fat body isozymes are clearly distinguishable by PAGE, and by pH optima and Michaelis constants.
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