alpha-Actinin and tropomyosin interactions with a hybrid complex of erythrocyte-actin and muscle-myosin.
alpha-Actinin isolated from dog muscle was used to incite antibodies in rabbits, Antibodies, purified by affinity chromatography on CNBr-Sepharose coupled with alpha-actinin and then ferritin-labeled were found to localize on the Z disc of muscle sarcomeres. Molecules of alpha-actinin as an adsorbed monolayer on the surface of polystyrene Lytron particles could bind muscle-actin and tropomyosin from solution. Both the ATPase activity and superprecipitation of an erythrocyte-actin and muscle-myosin hybrid actomyosin complex were altered by alpha-actinin, while tropomyosin diminished these alpha-actinin effects. The binding properties of alpha-actinin are consistent with those of an anchoring protein for microfilaments in nonmuscle cells.
D000185:Actinin; D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D004285:Dogs; D004789:Enzyme Activation; D004912:Erythrocytes; D006801:Humans; D005779:Immunodiffusion; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D008854:Microscopy, Electron; D009124:Muscle Proteins; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D014335:Tropomyosin
D000199:Actins; D046911:Macromolecular Substances; D009124:Muscle Proteins; D014335:Tropomyosin; D000185:Actinin; D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium