Piedimonte G, Silvotti L, Chamaret S, Borghetti A F, Montagnier L
J Cell Biochem. 1986;32(2):113-23. doi: 10.1002/jcb.240320204.
A tyrosine protein kinase activity has been detected in the mitochondrial fraction purified from human fibroblasts. By enzymatic and sedimentation analysis this activity appeared to be localized in the mitochondrial outer membrane. Mitochondrial tyrosine phosphorylation was strictly dependent on the presence of Mn2+ ions. An inverse relationship between cell proliferation and mitochondrial protein phosphorylation on tyrosine residues has been found: a marked increase in the mitochondrial tyrosine kinase activity occurred when a significant reduction in the growth rate followed serum step-down. In mitochondria purified from resting cells, a protein band with apparent molecular weight of 50 kd appeared to be phosphorylated on tyrosine.
在从人成纤维细胞中纯化得到的线粒体组分中检测到了酪氨酸蛋白激酶活性。通过酶促分析和沉降分析，该活性似乎定位于线粒体外膜。线粒体酪氨酸磷酸化严格依赖于Mn2+离子的存在。已发现细胞增殖与线粒体蛋白酪氨酸残基磷酸化之间呈负相关：当血清浓度降低后生长速率显著下降时，线粒体酪氨酸激酶活性显著增加。在从静止细胞中纯化得到的线粒体中，一条表观分子量为50 kd的蛋白条带似乎在酪氨酸上发生了磷酸化。
