Abstract
Phosphorylase kinase, a large oligomer of the composition α4 β4 γ4, is the key enzyme for the regulation of glycogen degradation. It catalyzes, activated by low concentration of Ca2+ ions, the conversion of Phosphorylase b to a, i.e. the phosphorylation of one specific serine residue of each of the two subunits of Phosphorylase b (1). In addition this kinase incorporates phosphate into its own subunit α (2, 3, 4) and into troponin (5). Fluoresceineisothiocyanate labelled antibodies against Phosphorylase kinase stain the sarcolemma and the sarcoplasmic reticulum of striated muscle 4cells (4, 6, 7, 8). These immunological results indicate the presence of this enzyme in membraneous structures. This paper will further demonstrate that this kinase in combination with a phosphatase influences the Ca2+ transport ATPase.
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References
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Hörl, W.H., Heilmeyer, L.M.G. (1977). Effect of a Ca2+ dependent protein kinase and a protein phosphatase on the Ca2+-phosphate transport ATPase. In: Massry, S.G., Ritz, E. (eds) Phosphate Metabolism. Advances in Experimental Medicine and Biology, vol 81. Springer, New York, NY. https://doi.org/10.1007/978-1-4613-4217-5_39
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DOI: https://doi.org/10.1007/978-1-4613-4217-5_39
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