Tóth G, Gergely P, Parsadanian H K, Bot G
Acta Biochim Biophys Acad Sci Hung. 1977;12(4):389-98.
The inhibitory effect of a heat-stable regulator protein from skeletal muscle on the activity of phosphorylase-phosphatase (EC 3.1.3.17) was studied. The regulator protein was shown to be both phosphorylated and dephosphorylated in vivo as well as in vitro. The incorporation of phosphate into the regulator protein increased, while dephosphorylation decreased the ability of the protein to inhibit phosphatase activity. Our results suggest that the reversible phosphorylation of the regulator protein plays an essential role in the regulation of phosphorylase-phosphatase activity.
研究了来自骨骼肌的一种热稳定调节蛋白对磷酸化酶磷酸酶（EC 3.1.3.17）活性的抑制作用。结果表明，该调节蛋白在体内和体外均可发生磷酸化和去磷酸化。调节蛋白中磷酸的掺入增加，而去磷酸化则降低了该蛋白抑制磷酸酶活性的能力。我们的结果表明，调节蛋白的可逆磷酸化在磷酸化酶磷酸酶活性的调节中起重要作用。
