Demonstrates that the light chain fraction of myosin from vertebrate skeletal muscle separates into four bands under specific electrophoretic conditions.
Four-band urea separation reveals myosin light chain heterogeneity in skeletal muscle; leaves open relevance to cardiac isoforms or function.
It is now widely accepted that the light chain fraction of myosin from rabbit skeletal muscle migrates as three bands on electrophoresis in the presence of sodium dodecyl sulfate (Paterson and Strohman, 1970; Starr and Offer, 1971; Weeds and Lowey, 1971). Our determinations indicate that these bands correspond to mol wts of 15,500, 18,500, and 22,500. Upon electrophoresis in 8 m urea at pH 8.6, however, the light chain fraction can be separated into four bands (Fig. 1). Similar observations with myosin from other species indicated that this was a general phenomenon for vertebrate skeletal muscle (Perrie and Perry, 1970).
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Perrie et al. (1973) studied this question.
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