Resolution of myocardial myosin light chains by two dimensional gel electrophoresis

Two dimensional gel electrophoresis of canine myocardial light chains of myosin demonstrated the existence of a single polypeptide species corresponding to the lighter component, C₂. However, contrary to previous observations, it was found that the heavier polypeptide, C₁, although homogeneous by one dimensional electrophoresis in polyacrylamide gels containing dodecyl sulfate, is resolved into 4 components by two dimensional gel electrophoresis at pH 8.7 and 4.5. Of these 4 components 2, named C1c and C1d, present in roughly equal amounts, comprise approximately 95% of the total C1 fraction, while the remaining 5% of the C₁ material consists of 2 components, named C1a and C1b.