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Accessibilité, solubilité et association,in situ, de la myosine

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Summary

β myosinin situ is the more accessible to saline solutions the more finely the muscular substance has been divided, which implies its localization in structures difficult of access.

This myosin exists in such structures in the form of a complex, the dissociation of which is effected by the saline solutions in proportion to their ionic strength.

Fatigue does not modify the spatial accessibility of this complex but does modify its structures, so that, for some values ofp H, solutions of equal ionic concentrations are less active on the substance of stimulated muscles than on that of normal ones.

Theβ myosin derived from that complex is much less homogenous in the Tiselius-Longworth apparatus than theβ myosin isolated from theWeber-Edsall myosin by fractionating with ammonium sulfate.

Rabbits' muscles suddenly cooled by immersion in ice water give extracts similar to those of stimulated muscles.

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References

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Authors and Affiliations

  1. Laboratoire de biologie générale, Faculté des sciences, Université de Liége, Belgium

    M. Dubuisson

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  1. M. Dubuisson
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Dubuisson, M. Accessibilité, solubilité et association,in situ, de la myosine. Experientia 3, 372–374 (1947). https://doi.org/10.1007/BF02154724

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