A New Myofibrillar Protein Characteristic of Type I Human Skeletal Muscle Fibres

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Abstract
Analysis of a single human type I (slow-twitch) skeletal muscle fibres by two-dimensional gel electrophoresis shows that they contain a specific protein of subunit M, 34 × 103 and PI 6.0,6.1 and 6.2 (three spots) which is absent from type IIA and IIB muscle fibres. This type I protein is located in the I-band of isolated myofibrils as demonstrated by the indirect immunofluorescence using specific antisera against the denatured form of type I protein. Type I protein could only be extracted from myofibrils with high salt solutions (0.6 - 1 M KCl), conditions which also coextract actin and myosin, demonstrating its firm attachment. Rat and cat type I muscle fibres as well as the slow-tonic fibres from chicken anterior latissimus dorsi also contained a protein homologous to the human type I protein. The human type I protein was found to be different from the known regulatory and contractile muscle proteins by electrophoretic and immunological criteria, and may therefore be a new myofibrillar protein in type I muscle fibres.