Measurement of ATPase activity of immobilized myosin heads.
Myosin, heavy meromyosin, and myosin subfragment-1 (S-1) were immobilized on the inner surfaces of glass capillary tubes, the inside walls of which had been coated with nitrocellulose. The ATPase activities of the immobilized proteins were measured using radiolabeled ATP and electrophoretic separation of the reaction products. The activity was proportional to the amount of immobilized protein. Activation by actin of the ATPase was also observed.
Hayashi
H
H
Department of Molecular Biology, School of Science, Nagoya University, Aichi.
Takiguchi
K
K
Higashi-Fujime
S
S
D000199:Actins / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000032:analysis / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D006868:Hydrolysis; D015879:Myosin Subfragments; D009218:Myosins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D010710:Phosphates / Q000302:isolation & purification; D010761:Phosphorus Radioisotopes
D000199:Actins; D004800:Enzymes, Immobilized; D015879:Myosin Subfragments; D010446:Peptide Fragments; D010710:Phosphates; D010761:Phosphorus Radioisotopes; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins