Lovell S J, Winzor D J
Biochem J. 1976 Sep 1;157(3):699-704. doi: 10.1042/bj1570699.
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.
兔肌肌浆球蛋白已在pH7.7、离子强度I = 0.05的0.0187M磷酸钾缓冲液中进行了移动界面电泳和速度沉降分析。上升和下降电泳图谱的非对映性足以表明肌浆球蛋白溶液中存在快速、可逆的相互作用。然而，在速度沉降实验中未获得明显大分子缔合的证据。电泳中非对映性的来源已追溯到磷酸盐与肌浆球蛋白成分的相互作用，因此应将其视为糖酵解酶的混合物，而非复合物。
