Troponin I from human skeletal and cardiac muscles

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Abstract
Myofibrils from human skeletal muscle contained regulatory proteins exhibiting similar electrophoretic behavior to those present in rabbit skeletal muscle. All human skeletal muscles examined contained 2 forms of troponin I corresponding to forms already characterized in fast and slow rabbit muscle. Ratios of amounts of the 2 forms of troponin I in different human skeletal muscles were not identical with ratios for the type 1 to type 2 fibers previously reported. Ratios were arranged in the same rank order. Primate heart contained a single form of troponin I different in MW and amino acid composition from skeletal forms. A monospecific antiserum to human cardiac troponin I was prepared in the sheep and did not react with fast or slow skeletal-muscle forms of troponin I from human and other species. The anti-(human cardiac-muscle troponin I) reacted with the cardiac troponin I from the human, baboon, rabbit and rhesus monkey. Positive reactions were obtained with urea extracts of whole cardiac tissue.