Salvatori S, Furlan S, Meggio F
CNR Centro di Studio per la Biologia e la Fisiopatologia Muscolare, Biomediche Sperimentali, Università di Padova, Italy.
Biochem Biophys Res Commun. 1994 Jan 14;198(1):144-9. doi: 10.1006/bbrc.1994.1021.
Calsequestrin from different muscle tissues and species has been phosphorylated by casein kinase-1 and casein kinase-2, in the conditions previously reported by Cala and Jones (J. Biol. Chem. 266, 391-398, 1991). Results indicates that rabbit cardiac and skeletal calsequestrin and frog skeletal calsequestrin are phosphorylated by both casein kinase-1 and casein kinase-2, at variance with chicken skeletal calsequestrin which is a poor substrate for both enzymes. We also observed that chicken calsequestrin is able to inhibit phosphorylation of cardiac calsequestrin, as well as other specific substrates, when added together to the assay medium.
在卡拉和琼斯之前报道的条件下(《生物化学杂志》266卷,391 - 398页,1991年),来自不同肌肉组织和物种的肌集钙蛋白已被酪蛋白激酶-1和酪蛋白激酶-2磷酸化。结果表明,兔心肌和骨骼肌肌集钙蛋白以及蛙骨骼肌肌集钙蛋白可被酪蛋白激酶-1和酪蛋白激酶-2磷酸化,这与鸡骨骼肌肌集钙蛋白不同,后者是这两种酶的不良底物。我们还观察到,当将鸡肌集钙蛋白与检测培养基一起添加时,它能够抑制心肌肌集钙蛋白以及其他特定底物的磷酸化。