Summary
Saline extracts from rabbit's skeletal muscles obtained and dialyzed at the ionic strength 0.15 contain at least 11 electrophoretically distinct components. Five of these components (n, m, t, l, s) have properties which are comparable with some characteristics of the myogens ofWeber, another component (h) is probably myoalbumin. Muscular proteins which are more soluble at higher ionic strength are not homogenous: there must be not one but two or more electrophoretically different myosins. Much work is needed to establish accurate relations between electrophoretic and classical muscular proteins.
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Literatur
M. Dubuisson etJ. Jacob, Rev. biol. Canad.4, 426 (1945).
Un diagramme obtenu à l'un de cespH a déjà été publié dans une notice précédente (M. Dubuisson etJ. Jacob, Exper.1, 273, fig. 2B) (1945).
H. H. Weber, Ergebn. Physiol.36, 109 (1934).
B. Smith, Proc. Roy. Soc.124, 136 (1937).
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Jacob, J. Electrophorèse de protéines musculaires de Lapin. Experientia 2, 110–111 (1946). https://doi.org/10.1007/BF02172572
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DOI: https://doi.org/10.1007/BF02172572