Hong S O, Ahn J Y, Lee C S, Kang M S, Ha D B, Tanaka K, Chung C H
Department of Molecular Biology, College of Natural Sciences, Seoul National University, Korea.
Biochem Mol Biol Int. 1994 Mar;32(4):723-9.
The subunit patterns of the proteasomes, that were purified from muscle, liver and brain, were found to be significantly different from one another. Furthermore, the proteasomes from adult and embryonic tissues of the same types also differed from each other in their subunit patterns. In addition, the specific activities of the purified proteasomes for peptide-cleavage, but not for casein-hydrolysis, appeared to be varied among the enzymes isolated from the different tissues. Thus, expression of a large number of proteasome subunits appears to be tissue-specific and under developmental control, although its relation with the multicatalytic activities of the proteasomes remains unclear.
从肌肉、肝脏和大脑中纯化得到的蛋白酶体的亚基模式，被发现彼此之间存在显著差异。此外，相同类型的成年组织和胚胎组织中的蛋白酶体，其亚基模式也互不相同。另外，纯化后的蛋白酶体对肽裂解的比活性（而非对酪蛋白水解的比活性），在从不同组织分离得到的酶之间似乎有所不同。因此，尽管蛋白酶体的大量亚基的表达与蛋白酶体的多催化活性之间的关系尚不清楚，但大量蛋白酶体亚基的表达似乎具有组织特异性且受发育调控。
