An effect of avian hereditary muscular dystrophy on the reaction of troponin-C with its antibody.
Antibody prepared against troponin-C, the calcium binding component of the troponin complex, was reacted with I band segments, and the distribution of antibody binding was assessed by immuno-electron microscopy. The I segments were isolated from glycerinated pectoral muscle which was prepared from normal adult chickens and from dystrophic chickens of strain 308. The antibody was deposited at 384 A +/- 7 A intervals along the thin filaments of the normal muscle. In contrast to the normal controls the dystrophic muscle did not exhibit a distinct periodicity when reacted with anti-troponin-C. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed that although protein bands corresponding to troponin-C could be observed in the gels of the dystrophic preparations, the troponin-C band had migrated slower than that from normal thin filaments. It is concluded that avian muscular dystrophy produces an alteration of the structure of troponin-C resulting in (1) an inability of the protein to combine with its specific antibody and (2) a change in its electrophoretic behavior.
D000818:Animals; D000937:Antigen-Antibody Reactions; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis*; D009137:Muscular Dystrophy, Animal / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D014336:Troponin / Q000032:analysis* / Q000276:immunology
D009124:Muscle Proteins; D014336:Troponin