Mohammad M A, Sparrow M P
Department of Physiology, University of Western Australia, Nedlands.
FEBS Lett. 1988 Feb 8;228(1):109-12. doi: 10.1016/0014-5793(88)80596-9.
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.
在4%十二烷基硫酸钠聚丙烯酰胺凝胶上进行电泳后，已测定猪气管平滑肌中肌球蛋白重链（MHCs）的化学计量。迁移较慢的MHC与迁移较快的MHC的比例在新生猪中为2.1，幼猪中为1.5，老年猪中为0.95（P小于0.01），表明MHC组成随发育而变化。MHCs的不等比例与Rovner等人[（1986年）《美国生理学杂志》250卷，C861 - 870页]早期提出的天然分子中MHCs的异二聚体排列不相符，提示天然分子可能由同二聚体重链组成。
