Dong S S, Stransky G I, Whitaker C H, Jordan S E, Schlesinger P H, Edwards J C, Blair H C
Department of Pathology, University of Alabama, Birmingham 35294-0007, USA.
Biochim Biophys Acta. 1995 Aug 16;1251(1):69-73. doi: 10.1016/0167-4838(95)00103-2.
Overlapping cDNA fragments encoding avian cathepsin B were cloned from an osteoclast cDNA library and sequenced. The primary structure of the prepro enzyme deduced from this sequence has 340 amino acids. The mature portion of the enzyme is 80% identical with murine cathepsin B; regions found in other papain superfamily enzymes are conserved. In osteoclasts and cultured macrophages, which produce large quantities of cathepsin B, mRNAs of 1.8 and 2.4 kb are produced in approximately equal quantities, while cells producing smaller quantities of the enzyme produce predominantly the 2.4 kb form. This variation in mRNAs suggests transcriptional differences related to production of large quantities of the enzyme.
从破骨细胞cDNA文库中克隆出编码禽组织蛋白酶B的重叠cDNA片段并进行测序。根据该序列推导的前原酶一级结构有340个氨基酸。该酶的成熟部分与鼠组织蛋白酶B有80%的同源性;在其他木瓜蛋白酶超家族酶中发现的区域是保守的。在产生大量组织蛋白酶B的破骨细胞和培养的巨噬细胞中,1.8 kb和2.4 kb的mRNA产生量大致相等,而产生该酶量较少的细胞主要产生2.4 kb形式的mRNA。mRNA的这种差异表明与大量产生该酶相关的转录差异。