The study identifies new large-size titin species (>3700 kDa) as the intact isoforms, suggesting previously known bands are fragments.
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May prompt re-evaluation of titin isoform models in sarcomeres; leaves open functional relevance in human cardiac disease.
By our modified SDS gel electrophoresis and immunoblotting, the isoform composition of titin in skeletal and cardiac muscles of human and animals was studied to reveal new titin forms above 3700 kDa in size. The data obtained suggest that the new large-size titin species are the intact (original) isoforms of this protein, whereas the known N2A, N2B, and N2BA titin bands in electrophoregrams correspond to their fragments.
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Vikhlyantsev et al. (2006) studied this question.
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