Rabbit muscle myogen has been subjected to moving-boundary electrophoresis and velocity sedimentation in 0.0187 M-potassium phosphate buffer, pH7.7, I = 0.05. The ascending and descending 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 velocity-sedimentation experiments. The source of the non-enantiography in electrophoresis has been traced to interactions of phosphate with components of myogen, which should therefore be considered as a mixutre, rather than a complex, of glycolytic enzymes.
Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis
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S J Lovell, D J Winzor; Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis. Biochem J 1 September 1976; 157 (3): 699–704. doi: https://doi.org/10.1042/bj1570699
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