Changes in myosin heavy chain stoichiometry in pig tracheal smooth muscle during development.
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 neonates, 1.5 in young and 0.95 in old pigs (P less than 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.
Mohammad
M A
MA
Department of Physiology, University of Western Australia, Nedlands.
Sparrow
M P
MP
D000818:Animals; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D024510:Muscle Development; D009130:Muscle, Smooth / Q000032:analysis* / Q000254:growth & development; D015879:Myosin Subfragments; D009218:Myosins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D013552:Swine; D014132:Trachea / Q000032:analysis / Q000254:growth & development
D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins