Abstract
Scallop adductor muscle β-like isoactin differs from rabbit skeletal muscle α-actin in the rate, extent and critical concentration of polymerization. The difference is temperature- and [KCl]-dependent. In the presence of DNase I scallop actin was shown to be depolymerized more rapidly than rabbit actin. It was suggested that the polymers formed by β-actin are less stable than those formed by α-actin.
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