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

Abstract

Rabbit muscle myogen has been subjected to moving-boundary electrophoresis and velocity sedimentation in 0.0187M-potassium phosphate buffer, pH7.7, I=0.05. The ascending and descending electrophoretic patterns are sufficiently non-enantiographic to suggest the existence of rapid, reversible interactions in the myogen solutions. However, no evidence of pronounced macromolecular association was obtained in velocitysedimentation experiments. The source of the non-enantiography in electrophoresis has been traced to interactions ofphosphate with components ofmyogen, which should therefore be considered as a mixture, rather than a complex, of glycolytic enzymes.