Affinity chromatography of myosin, heavy meromyosin, and heavy meromyosin subfragment one on F-actin columns stabilized by phalloidin

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Abstract
A method of affinity chromatography based on the trapping of actin filaments within agarose gel beads is described. This method was used for the purification of myosin and its active proteolytic subfragments and for studies on the interaction between actin and these proteins. Actin columns stabilized by phalloidin are myosin, heavy meromyosin (HMM) and HMM-subfragment 1 (HMM-S1) specifically and reversibly. The effect of PPi and KCl on the dissociation of actomyosin, acto-HMM or acto-HMM-S1 complex is reported. The single-step purification of myosin from a crude rabbit psoas muscle extract is also described.