The location of the single cysteinyl residue of the alkali light chain on the myosin head was determined by electron microscopy. The cysteinly residue of isoloated alkali light chain 2 was biotinylated and the light chain was exchanged with that of heavy meromyosin in 4-7 m-NH4Cl. Avidin was attached to the biotin in the heavy meromyosin and the complex was rotary shadowed and observed in the electron microscope. The distance from the head-rod junction to the centre of avidin was 8(±3)nm (mean value ± standard deviation:n=105).
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