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A chromatographic system using DEAE-Sephadex A-50 with 0.04 m pyrophosphate buffer, pH 7.5, and a linear KC1 gradient to 0.50 m KC1 separates monomeric myosin from aggregated myosin, other unidentified proteins, and ribonucleic acid (RNA).The procedure has been applied to myosin preparations from skeletal muscle of rabbit, chicken, and K-zeveral investigators have employed column chromatography for the purification of myosin. Brahms (1959) and Perry (1960) used DEAE-cellulose with 0.2 m KC1 buffered with Tris to pH 7.4, and obtained some degree of fractionation, but the bulk of the material passed directly through the column without retention. Perry (1960) also employed a buffer system (0.16 m KC1-0.02 m Tris, pH 8.2) with a KC1 gradient that resulted in a separation of myosin from ribonucleoprotein and other proteins that passed through unretarded. However, the adenosine triphosphatase (ATPase)* 1 **activity varied considerably across the myosin peak, and dimers not present in the starting material were seen in the myosin purified by this procedure. Based on the work of Brahms and Brezner (1961), who showed that myosin was soluble in polyphosphates at low ionic strength, Asai (1963) used DEAE-cellulose columns, ATP in the solvent, and a KC1 gradient to obtain chromatograms that were similar to those obtained with the pH 8.2 system of