A new preparation of actin from Dictyostelium discoideum showed similar properties to muscle actin and formed longer filaments than previous preparations.
A new purification procedure for Dictyostelium actin yields 5-10 times more protein and produces longer filaments compared to previous methods, closely resembling rabbit skeletal muscle actin.
Actin has been purified from amoebae of Dictyostelium discoideum by a procedure which is notable in that proteolysis has been diminished to undetectable levels and "selective" purification steps have been avoided. The overall yield of this procedure is 5- to 10- fold greater than that of a previous report (Spudich, J. A. (1974) J. Biol. Chem. 249, 6013-6020). The detailed biochemical and structural properties of this new preparation (preparation B) have been compared to those of Dictyostelium actin prepared by the previous procedure (preparation A) as well as to rabbit skeletal muscle actin. Preparation B actin is similar to muscle actin in its molecular weight, ability to activate myosin, filament structure, and polymerization properties. Preparation B actin has the same molecular weight and isoelectric point as preparation A actin, which is more acidic than that of skeletal muscle actin. However, preparation B actin and muscle actin form longer filaments than preparation A actin, as judged by viscometry and electron microscopy.
Uyemura et al. (Fri,) reported a other. Preparation B actin (new preparation) vs. Preparation A actin and rabbit skeletal muscle actin was evaluated on Biochemical and structural properties (molecular weight, myosin activation, filament structure, polymerization). A new preparation of actin from Dictyostelium discoideum showed similar properties to muscle actin and formed longer filaments than previous preparations.
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