alpha-Actinin and tropomyosin interactions with a hybrid complex of erythrocyte-actin and muscle-myosin
Autor: | William Schook, Elena Puszkin, Saul Puszkin, Richard E. Rosenfield, Christine Ores, Charles Rouault, Jonathan Maimon, Shaul Kochwa |
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Rok vydání: | 1977 |
Předmět: |
Immunodiffusion
Erythrocytes Macromolecular Substances Protein Conformation Muscle Proteins Tropomyosin macromolecular substances Actinin Myosins Biology Microfilament Biochemistry Sarcomere Dogs Affinity chromatography Myosin Animals Humans Magnesium Molecular Biology Actin Adenosine Triphosphatases Muscles Cell Biology musculoskeletal system Actins Rats Enzyme Activation Kinetics Microscopy Electron Actinin alpha 1 Biophysics Protein Binding |
Zdroj: | Journal of Biological Chemistry. 252:5529-5537 |
ISSN: | 0021-9258 |
Popis: | 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. |
Databáze: | OpenAIRE |
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