Polymerization of beta-like actin from scallop adductor muscle.

Scallop adductor muscle beta-like isoactin differs from rabbit skeletal muscle alpha-actin in the rate, extent and critical concentration of polymerization. The difference is temperature- and [KC1]-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 beta-actin are less stable than those formed by alpha-actin.