Analysis of structural proteins from biopsied human myocardium with special emphasis on methodology.

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Abstract
An analytical procedure for the quantitative determination of the structural proteins from a biopsied human cardiac muscle weighing approximately 1 mg was described to be applicable in clinical studies in 20 patients with various heart diseases. The principle of the method is glycerinization of heart muscle and analysis by SDS [sodium dodecyl sulfate] gel electrophoresis. In 6 control heart muscles obtained from patients having almost normal hearts, the pattern of the structural proteins was similar to that of the normal canine heart. Myosin heavy chainactin ratio ranged 1.26 .+-. 0.44. In 5 cases with secondary cardiac hypertrophy, the pattern of the structural proteins was the same as that of the control heart. In 4 cases with hypertrophic cardiomyopathy, an increase in myosin heavy chain was observed in 2 cases, while myosin heavy chain and .alpha.-actinin decreased in another 2 cases. Hypertrophy and severe disarray of myofibrils were noted in the former, and atrophy and degradation were done in the latter in EM. In 5 cases with diluted cardiomyopathies, the relative contents of myosin heavy chain and .alpha.-actinin was reduced in all cases together with atrophy and degradation of myofibrils.