ABSTRACTThe chicken breast muscle proteins myosin, actin and synthetic acto‐myosin (SAM) were taken to 0.6M NaCl, 20 mM citrate‐phosphate buffer, pH 5.5–7.0, and were tested for emulsifying capacity (E.C.) and timed emulsification. The aqueous phase was separated by centrifugation and analyzed quantitatively by SDS gel electrophoresis. Emulsifying capacity values varied inversely with protein concentration and pH, with myosin ≅ SAM (+ ATP)>SAM (− ATP)>actin. However, oil phase volume differences were small, ranging from 86.5–88.7. The proteins actin and myosin had quite different emulsion‐forming properties. Myosin was rapidly removed from solution, forming fine, thick emulsions. Actin was less readily removed from solution, and formed thin, coarse emulsions. When present as actomyosin, actin and myosin behaved like myosin alone. However, when this complex was dissociated by ATP (5 mM), actin and myosin behaved independently of each other. Actin remained in the aqueous phase while myosin was preferentially used in
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