Summary
The fine structural morphology and the ATP-ase activity of heart muscle at various sarcomere lengths was studied. ATP-ase activity was found on endothelial cells, cell membrane, intercalated disc, sarcoplasmic reticulum and in the Z-line region. It appeared that the activity of the ATP-splitting in the Z-line region was sensitive to PCMB and could be reactivated with cysteine. This points to an activity of “true” ATP-ase according to the terminology ofPadykula et al. (1955) andFreiman et al. (1960). In addition, this cross striational enzyme was strongly activated by Mg++.
At intermediate sarcomere lengths and in hypercontraction no I-zones or H-zones were visible, while at intermediate sarcomere lengths and M-line was faintly indicated. In the stretched muscle, both I- and H-zones and N- and M-lines were present. In comparison with muscle tissue with intermediate sarcomere lengths, the Cz-bands of hypercontraction had markedly broadened, whereas in stretched muscle a relatively sharply defined electron-dispersing line indicated the presence of a Z-line.
The localization and spread of the precipitate formed as a result of ATP-ase activity changes with alterations of the sarcomere lengths exclusively in the Z-line region.
The probable identity of the Z-line region ATP-ase with Actomyosin is discussed.
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de Man, J.C.H., de Beyer, J.M. & Persijn, J.P. Fine structural morphology and ATP-ase reaction in heart muscle at various sarcomere lengths. Histochemie 3, 269–282 (1963). https://doi.org/10.1007/BF00736444
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DOI: https://doi.org/10.1007/BF00736444