Demonstrates that beta-actin polymers from scallop adductor muscle are less stable than alpha-actin polymers from rabbit skeletal muscle.
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No immediate clinical implications; extends comparative actin biology but leaves open human cardiac relevance.
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.
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Sofia Khaitlina (1986) studied this question.
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