Kazakova T B, Mel'nikova M P, Sverdlov E D
Mol Cell Biochem. 1977 Feb 4;14(1-3):37-45. doi: 10.1007/BF01734163.
Specific sites that interact with structural proteins of the mitochondrial inner membrane were found in mitochondrial DNA (mtDNA) of rat liver. Analysis of the isolated DNA fragments revealed their capacity to form a complex with membrane proteins in vitro and allowed the detection of a protein with a molecular weight 40,000. The size of the fragments was found to be 12-18 nucleotide pairs with an average molecular weight 10,000 MtDNA sites recognized by membrane protein proved to be quite unique in having a secondary structure, a high content of AT sequences (82%) and oligopyrimidine blocks. It was shown that the light mtDNA strand, rich in adenine, is 60% more active in the binding with membrane mitochondria than the heavy one.
在大鼠肝脏的线粒体DNA（mtDNA）中发现了与线粒体内膜结构蛋白相互作用的特定位点。对分离出的DNA片段进行分析，结果显示它们在体外能够与膜蛋白形成复合物，并且检测到一种分子量为40,000的蛋白质。发现这些片段的大小为12 - 18个核苷酸对，平均分子量为10,000。被膜蛋白识别的mtDNA位点在具有二级结构、高含量的AT序列（82%）和寡嘧啶区段方面表现得相当独特。结果表明，富含腺嘌呤的轻链mtDNA与线粒体膜结合的活性比重链高60%。
