An effect of avian hereditary muscular dystrophy on the reaction of troponin-C with its antibody |
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Authors: | Mary J Irish Tamio Hirabayashi Frank J Wilson |
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Institution: | 1. Department of Anatomy, College of Medicine and Dentistry of New Jersey, Rutgers Medical School, Piscataway, New Jersey 08854, U.S.A.;2. Zoological Institute, Tokyo Kyoiku University Otsuka 3-29-1, Bunkyo-ku, Tokyo, Japan |
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Abstract: | 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 Å ± 7 Å 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. |
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