Changes in myosin heavy chain stoichiometry in pig tracheal smooth muscle during development

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Abstract
The stoichiometry of the myosin heavy chains (MHCs) has been measured in the tracheal smooth muscle of the pig after electrophoresis on SDS 4% polyacrylamide gel. The ratio of slower migrating MHC to the faster migrating MHC was 2.1 in neonates, 1.5 in young and 0.95 in old pigs (P<0.01) showing that MHC composition changes with development. The unequal proportion of MHCs was not compatible with a heterodimeric arrangement of the MHCs in the native molecule as proposed earlier by Rovner et al. [(1986) Am. J. Physiol. 250, C861–870] and it is suggested that native molecules may be composed of homodimer heavy chains.