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- W2073389885 abstract "Abstract 1. 1. The viscosity, the intensity of flow birefringence, and the rotary diffusion constant of myosin B, prepared from rabbit skeletal muscle, were investigated over a wide range of the velocity gradient (17–12,500 sec−1). The following results were obtained. 2. 2. The viscosity decreased with increase of the gradient. 3. 3. At low gradient myosin B particles behaved polydispersedly with respect to the rotary diffusion, while at high gradient they were monodisperse. The rotary diffusion constant increased with increment of the gradient, and at sufficiently high gradient it was a constant value (ca. 20 sec−1), independent of gradient and the protein concentration. 4. 4. The length of the equivalent elongated ellipsoid calculated from the rotary diffusion constant at sufficiently high gradient was 8,600–10,100 A, in satisfactory agreement with results obtained from light scattering. 5. 5. At a low range of gradient ( 6. 6. If the protein solution were once subjected to a high gradient, the intensity of flow birefringence observed at low gradient was considerably higher than the original value. 7. 7. In high KCl solution, the rotary diffusion constant was observed to be higher than 10 sec−1 even at a low range of gradient. 8. 8. Consequently, it was concluded that a network is built up by the electrostatic interferences of the constituent elementary particles with each other and the entanglements are broken more and more as the gradient increases, that the length of the elementary particles is almost constant, and that the orientation of polypeptide chains in these particles is improved by high shearing stress. 9. 9. The rotary diffusion constant at high shearing stress increased remarkably on the addition of ATP. The molecular mechanism of this effect was briefly discussed." @default.
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- W2073389885 date "1958-01-01" @default.
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- W2073389885 title "Rotary diffusion of actomyosin" @default.
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- W2073389885 doi "https://doi.org/10.1016/0006-3002(58)90337-8" @default.
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