Sarrouilhe D, Baudry M
Groupe de Recherche et d'Etude d'Analogues de Médicaments, Faculté de Médecine et de Pharmacie, Poitiers, France.
Cell Mol Biol (Noisy-le-grand). 1996 Mar;42(2):189-97.
A true protein kinase CKII (CKII) activity was characterized in liver mitochondria by its phosphorylating activity on the specific peptide substrate of CKII, the binding and elution profile of the enzyme on a phosphocellulose column and immunostaining of a 36 kDa polypeptide with antibodies against the alpha-subunit of human CKII. This CKII activity was located predominantly in the intermembrane space of quiescent mitochondria. A translocation of the enzyme to inner membrane of energized mitochondria occurred in the presence of spermine. Translocated CKII activity was tightly bound to inner membrane, and high salt concentrations were necessary to release the activity. The inner face of the inner membrane could constitute the in vivo localization of mitochondrial CKII since the potential substrates of the enzyme are 4 matrix proteins.
通过其对CKII特异性肽底物的磷酸化活性、该酶在磷酸纤维素柱上的结合与洗脱图谱以及用抗人CKIIα亚基抗体对36 kDa多肽进行免疫染色，在肝线粒体中鉴定出了真正的蛋白激酶CKII（CKII）活性。这种CKII活性主要位于静止线粒体的膜间隙。在精胺存在的情况下，该酶会转移到活跃线粒体的内膜上。转移后的CKII活性紧密结合在内膜上，需要高盐浓度才能释放该活性。内膜的内表面可能构成线粒体CKII在体内的定位，因为该酶的潜在底物是4种基质蛋白。
