AMOEBA actin, a protein that shares many of the chemical, physical, and ultrastructural properties of muscle actin, has recently been isolated from Acanthamoeba castellanii1,2. The final steps in the purification procedure are the sedimentation of polymerized amoeba F-actin, its depolymerization by prolonged dialysis against a solution of ATP, and separation by molecular filtration on ‘Sephadex G-200’ of a minor excluded fraction and a major included fraction (amoeba G-actin). The product is monodisperse as judged by sedimentation equilibrium centrifugation in 5 M guanidine1 and has a molecular weight of about 39,500. Polyacrylamide gel electrophoresis at pH. 9.5 in 8.5 M urea of the reduced, carboxymethylated protein shows one major band that accounts for more than 90 per cent of the stainable protein. The amino-acid composition of amoeba actin was found to be very similar to that of other act ins including approximately 1 mole of the rare amino-acid 3-methylhistidine (3-MH) per mole of protein1. In addition, an unidentified component was detected which had the same elution time as ε-N-methyllysine in the chromatographic system used1 which does not separate monomethyllysine from dimethyllysine.
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