Light chains of myosins from white, red, and cardiac muscles.

Purified preparations of rabbit skeletal white, red, and cardiac muscle myosin (WM, RM, and CM) were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Significant differences in both the molecular weights and number of light chains in these myosins were found. WM has three distinct light-chain components (LC(1W), LC(2W), LC(3W)) having molecular weights of 25,500, 17,400, and 15,100, respectively. No component with a molecular weight around 15,000 is present in RM or CM. RM and CM contain components of identical molecular weights close to 25,000 and 17,000 (LC(1CR) and LC(2CR)) which, however, clearly differ in molecular weight from the corresponding subunits in WM. RM has an additional component (LC(1R)) having a slightly higher molecular weight than LC(1W) and LC(1CR). Thus differences and similarities in many biochemical properties between WM, RM, and CM, which have been described earlier, are also reflected in the light-chain components. The present results support the hypothesis that different sets of genes are active in producing components of myosin that make up different isozymic forms characteristic of each muscle type.