Effect of calcium on extraction of Z-band proteins from I-Z-I brushes of rabbit striated muscle.
1. When rabbit striated muscle I-Z-I brushes were subjected to eleven extractions with three different extracting solutions, relatively more amount of proteins was extracted in the presence of 1 nM CaCl2 than in the presence of 5 mM EDTA or 5 mM ethyleneglycol-bisp(beta-aminoethylether)-N,N,N1,N1-tetra-acetic acid (EGTA). Among proteins extracted in the presence of 1 mM CaCl2, the protein components with molecular weights of 85,000, 95,000 and 220,000 were included, whereas these were not extracted in the other two. 2. Co-electrophoreses of 220,000 dalton protein and myosin heavy chain showed that these two protein components were distinct from each other. 3. Roles of Ca2+ are discussed on disintegration processes of I-Z-I brushes in special reference to its co-operative action with calcium-activated factor enzyme.
D000818:Animals; D002118:Calcium; D004492:Edetic Acid; D004533:Egtazic Acid; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification*; D009132:Muscles / Q000032:analysis* / Q000648:ultrastructure; D009218:Myosins / Q000302:isolation & purification; D011817:Rabbits
D009124:Muscle Proteins; D004533:Egtazic Acid; D004492:Edetic Acid; D009218:Myosins; D002118:Calcium