Dynamic Laser Light Scattering of Papain-Treated Thick Filaments from Limulus Striated Muscle in Suspension
Using quasielastic light scattering we have previously shown an increase in high frequency internal motion of isolated thick filament upon activation. This we have attributed to cross-bridge motion.Here we show that after cleavage of the S1 moiety of myosin from isolated filaments with papain, calcium ions no longer activate the isolated filaments to produce high-frequency motions.
KeywordsThick Filament Myosin ATPase Relaxing Solution Myosin Subfragment Dynamic Laser Light Scattering
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- Fan, S-F. and Wen, Y-S. (1979). Concerning the binding sites of myofibril with Congo Red and dichroism change with myofibril length of Congo Red stained glycerinated sartorius muscle fibers. Acta Physiol. Sinica. 31: 227–238.Google Scholar
- Goodno, C.C. and Taylor, E.W. (1982). Inhibition of actomyosin ATPase by vandate. ibid., 79: 21–25.Google Scholar
- Kubota, K., Chu, B., Fan, S-F., Dewey, M.M., Brink, P. and Colflesh, D. Quasi-elastic light scattering of suspensions of Lin - Lulus thick myofilaments in relaxed (long), activated and re-relaxed (short) states. Submitted to J. Mol. Biol.Google Scholar
- Yamanaotoik, K. and Schiao, T. (1980). Substructure of myosin subfragment (as revealed by digestion with proteolytic enzymes). J. Biochem. ( Tokyo ). 87: 219–226.Google Scholar