Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis.
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.
D000818:Animals; D004586:Electrophoresis; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D009124:Muscle Proteins / Q000302:isolation & purification; D010710:Phosphates; D011817:Rabbits; D014461:Ultracentrifugation
D009124:Muscle Proteins; D010710:Phosphates; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases