Abstract
Rabbit myosin prepared in the conventional manner by repeated precipitation at low ionic strength was previously shown to contain substantial amounts of impurities; the principal impurity is a component of the myofibril called C-protein. Because antiserum to such conventionally prepared myosin was previously used for labeling studies of muscle, it was necessary to study the immunological characteristics of myosin and C-protein, and in particular to test the specificity of this antiserum. Antisera to rabbit myosin and C-protein were successfully elicited in goats. These antisera were analyzed by immunodiffusion and by precipitin reactions in solution. The analysis was helped by the examination of immunoprecipitates by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate. C-protein and myosin are antigenically distinct, and thus C-protein is not derived from myosin. Purified myosin can behave as a classically simple antigen giving a single precipitin line when diffused against its homologous antiserum. C-protein is a powerful immunogen; the amount present as an impurity in myosin prepared in the conventional way by repeated precipitation at low ionic strength is capable of eliciting a large amount of antibody.

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