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Abstract The low molecular weight protein associated with rabbit skeletal myosin has been estimated by gel filtration studies in 5 m guanidine hydrochloride and was found to constitute 9 ± 2% of the myosin mass. We have found that 40 to 50% of the low molecular weight protein can be removed from myosin without any apparent changes in the adenosine-triphosphatase activity. Attempts to remove a larger fraction of low molecular weight protein resulted in a concomitant loss of enzymatic activity. The molecular weight of the major myosin subunit freed of low molecular weight protein has been redetermined in 5 m guanidine hydrochloride and was found to be 194,000 g per mole. The significance of its presence in assessing the molecular weight of the major subunit at low speed and high speed sedimentation equilibrium has been investigated.
Gazith et al. (1970) studied this question.