Piedimonte G, Chamaret S, Dauguet C, Borghetti A F, Montagnier L
Istituto di Patologia Generale, Università di Parma, Italy.
J Cell Biochem. 1988 Jan;36(1):91-102. doi: 10.1002/jcb.240360110.
Tyrosine protein kinase activity has been detected in the mitochondrial fraction purified from sarcoma 180 tumor cells. Following hypotonic disruption of mitochondria, tyrosine kinase activity appeared to cosediment with monamine oxidase, marker enzyme of mitochondrial outer membrane; meanwhile, serine and threonine kinases were found to be associated with the inner membrane and matrix of mitochondria. Mitochondrial tyrosine kinase(s) showed thermosensitivity and Mn2+ dependence, useful properties for its characterization and separation from tyrosine kinases associated with other particulate fraction and from serine and threonine kinases associated with mitochondria. Following in vitro incubation of mitochondria with labelled ATP as substrate and analysis by PAGE, a complex pattern of phosphotyrosine containing proteins with a major band of 50-55 kilodaltons resulted.
在从肉瘤180肿瘤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。线粒体经低渗破碎后，酪氨酸激酶活性似乎与单胺氧化酶（线粒体外膜的标志酶）共同沉降；与此同时，丝氨酸和苏氨酸激酶被发现与线粒体内膜和基质相关联。线粒体酪氨酸激酶表现出热敏感性和对Mn2+的依赖性，这对于其特性鉴定以及与其他颗粒组分相关的酪氨酸激酶和与线粒体相关的丝氨酸和苏氨酸激酶的分离而言是有用的特性。用标记的ATP作为底物对线粒体进行体外孵育并通过聚丙烯酰胺凝胶电泳分析后，得到了一个复杂的含磷酸酪氨酸蛋白图谱，其中主要条带为50 - 55千道尔顿。
