Chicken‐Gizzard Actin: Polymerization and Stability

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Abstract
Preparations of chicken gizzard actin obtained from acetone-dried muscle powders prepared with various methods developed for skeletal muscle contain variable amounts of a .beta.-actinin-like protein. This contamination is minimized if the procedure of muscle powder preparation includes washing with EDTA solution and can be completely removed by gel filtration of G-actin on Sephadex G-100. The presence of .beta.-actinin activity manifests itself in an increased rate of actin polymerization, low filament lengths resulting in low viscosity and enhanced ATP-splitting activity of actin polymer, and instability of the polymer in the absence of free ATP. Gizzard actin purified on a Sephadex G-100 column does not differ from rabbit skeletal muscle actin in its polymerization properties. The distinct property of gizzard actin is the instability of its G form in the absence of added Ca2+, indicating that the affinity of this cation for the single high-affinity site in gizzard actin is lower than in skeletal muscle actin.

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