Abstract
Cardiac troponin I, the inhibitory subunit of troponin, is phosphorylated in mammalian hearts upon β-adrenergic stimulation (England, 1975; Solaro et al., 1976). On rabbit troponin I it is believed to occur at serine-20 (Moir & Perry, 1977). In hormonally stimulated perfused hearts a correlation between phosphorylation of this single amino acid and change in contractility was expected which, however, could not be clearly demonstrated (Westwood & Perry, 1981). Freshly isolated troponin I from both rabbit and bovine heart contains 1.5–1.9 mol of phosphate per mol of protein (Cole & Perry, 1975; Swiderek et al., 1988) indicating that in addition to phosphoserine-20 a second phosphate residue of unknown location is bound in the N-terminal sequence (Moir & Perry, 1981). Recently, two adjacent phosphoserine residues in position 23 and 24 were identified in troponin I from bovine heart (Swiderek et al., 1988).
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References
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© 1991 Springer-Verlag Berlin Heidelberg
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Mittmann, K., Jaquet, K., Heilmeyer, L.M.G. (1991). Two Adjacent Phosphoserines in Bovine, Rabbit and Human Cardiac Troponin I. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_19
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DOI: https://doi.org/10.1007/978-3-642-75142-4_19
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