The possible role of myosin A1 light chain in the weakening of actin–myosin interaction

• Published in: Biochimica et biophysica acta Vol. 1340; no. 1; pp. 105 - 114
• Main Authors: St e ̧ pkowski, Dariusz, Efimova, Natalya, Paczyńska, Agnieszka, Moczarska, Anna, Nieznańska, Hanna, Kąkol, Irena
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 20.06.1997
• Subjects: Actin; Actins - metabolism; Actins - pharmacology; Adenosine Triphosphatases - metabolism; Animals; Binding Sites; Ca(2+) Mg(2+)-ATPase - metabolism; Calcium-Transporting ATPases - metabolism; Cation Transport Proteins; Kinetics; Myosin; Myosin alkali light chain; Myosin Light Chains - chemistry; Myosin Light Chains - physiology; Myosin Subfragments - metabolism; Myosins - metabolism; Osmolar Concentration; Papain - metabolism; Peptide Fragments - metabolism; Phosphorylation; Rabbits; Structure-Activity Relationship; Sulfhydryl Compounds - metabolism; Actin; Myosin alkali light chain; Myosin

The effects resulting from the removal of the N-terminus of myosin A1 by limited papain cleavage are investigated. The myosin and heavy meromyosin K +-ATPase and Ca 2+-ATPase activities, and actin-activated ATPase activity of heavy meromyosin (HMM) and subfragment-1, are studied. Myosin and HMM prep...