Abstract
IN vertebrate smooth muscle actomyosin can be extracted at low ionic strength as well as at high ionic strength. Attention was first directed to this by Laszt and Hamoir1 and later by Huys2, who found an actomyosin in vertebrate smooth muscle, soluble at low ionic strength (I = 0.1 and less) in the presence of 0.1 mM ATP, which they called tono-actomyosin. The sedimentation constant, electrophoretic mobility and relative viscosity with and without ATP of tono-actomyosin are all different from those of normal actomyosin, but after treatment of tono-actomyosin with potassium or sodium chloride of high ionic strength (I = 0.35) these values become the same as those of normal actomyosin.
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References
Laszt, L., and Hamoir, G., Biochim. Biophys. Acta, 50, 430 (1961).
Huys, J., Arch. Intern. Physiol. Biochim., 69, 677 (1961).
Elliott, G. F., Proc. Roy. Soc., B, 160, 467 (1964).
Choi, J. K., Fifth Intern. Congr. Electron Microscopy, Philadelphia, M9 (1962).
Needham, D. M., and Shoenberg, C. F., Proc. Roy. Soc., B, 160, 523 (1963).
Huxley, H. E., J. Mol. Biol., 7, 281 (1963).
Hanson, J., and Lowy, J., Proc. Roy. Soc., B, 160, 523 (1963).
Hanson, J., and Lowy, J., J. Mol. Biol., 6, 46 (1963).
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SHOENBERG, C. Contractile Proteins of Vertebrate Smooth Muscle. Nature 206, 526–527 (1965). https://doi.org/10.1038/206526a0
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DOI: https://doi.org/10.1038/206526a0
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