Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis

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Abstract
Rabbit muscle myogen was subjected to moving-boundary electrophoresis and velocity sedimentation in 0.0187 M-potassium phosphate buffer, pH 7.7, I [ionic strength] = 0.05. The ascending and descending electrophoretic patterns are sufficiently non-enantiographic to suggest the existence of rapid, reversible interactions in the myogen solutions. No evidence of pronounced macromolecular association was obtained in velocity-sedimentation experiments. The source of the non-enantiography in electrophoresis was traced to interactions of phosphate with components of myogen, which should therefore be considered as a mixture, rather than a complex, of glycolytic enzymes.