Dianoux A C, Bof M, Vignais P V
Eur J Biochem. 1978 Jul 17;88(1):69-77. doi: 10.1111/j.1432-1033.1978.tb12423.x.
A product of mitochondrial protein synthesis in rat liver mitochondria, characterized by a low molecular weight (Mr is less than 10000) and an unusually high hydrophobicity, has been identified as the dicyclohexylcarbodiimide-binding protein and as a peptide of the hydrophobic sector of the mitochondrial ATPase complex. The purified protein still possesses the ability of bind dicyclohexylcarbodiimide.
在大鼠肝脏线粒体中由线粒体蛋白质合成产生的一种产物,其特点是分子量低(Mr小于10000)且疏水性异常高,已被鉴定为二环己基碳二亚胺结合蛋白以及线粒体ATP酶复合体疏水部分的一种肽。纯化后的该蛋白质仍具备结合二环己基碳二亚胺的能力。