Abstract

Nutritional muscular dystrophy in the chick results from the simultaneous deficiency of vitamin E and cystine. Being a biological antioxidant, vitamin E might be functional in maintaining a proper redox state of the sulfur-containing amino acid in the proteins. The analyses of protein-bound sulfhydryls and disulfides at onset of muscular dystrophy in young chicks were carried out. The ratio of disulfide to sulfhydryls increased two- to three-fold in dystrophic muscle as compared to that in the control muscle proteins. Dystrophic and normal muscle proteins also were subjected to SDS-gel electrophoresis. Proteins of low molecular weight, supposedly derived from proteolysis, were present in the gels of the dystrophic muscle and absent in those of normal muscle extracts. As a result of these studies, a chemical model has been proposed to explain the oxidative deterioration of proteins in nutritional muscular dystrophy due to vitamin E deficiency.

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