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.
D000199:Actins; D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D003850:Deoxyribonuclease I / Q000494:pharmacology; D007700:Kinetics; D008974:Mollusca; D009132:Muscles / Q000032:analysis; D011108:Polymers; D011189:Potassium Chloride / Q000494:pharmacology; D011817:Rabbits; D013696:Temperature
D000199:Actins; D011108:Polymers; D011189:Potassium Chloride; D003850:Deoxyribonuclease I