STUDIES ON THE PROTEINS OF SMOOTH MUSCLE

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Abstract
Myosins were prepared from the smooth muscles of Polynices lewisii and Polypus bimaculatus and studied by the method of double refraction of flow. The molecules were found about the same length as the myosins of the skeletal muscle of the rabbit and the cow. The effects of alkali and urea upon the double refraction of flow of the invertebrate myosin solns. were similar to those of vertebrate myosins. No myosin was obtained from Cribrina xantho-grammica or from Stichopus californicus. It is not known whether the negative finding indicates the absence of myosin, or the failure to extract it. Thus the optical differences between smooth and striated muscle do not depend, at least in certain cases, upon any essential differences in the structure of the proteins, but upon the arrangement of the protein molecules within the fibril.

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