Abstract
Proteins prepared from dystrophic muscles were studied by use of the ultracentrifuge in an attempt to characterize them by comparison with similar preparations from normal muscle. The extraction procedures and identification of protein components are described. The material obtained from normal human or goat muscle appeared to be a fairly homogenous preparation of myosin when studied in the ultracentrifuge at low temperature but the same procedure applied to human dystrophy muscle yielded polydisperse material. Myosin from vitamin E deficient rabbits precipitated at higher salt concentrations than myosin prepared from normal rabbit muscle. KI extracts of muscles of mice showing clinical signs of muscular dystrophy or of muscles from healthy mice gave ultracentrifuge patterns similar to those seen in the case of human dystrophy material. The possible significance of these findings is discussed.

This publication has 2 references indexed in Scilit: