Dahlmann B, Kopp F, Kuehn L, Hegerl R, Pfeifer G, Baumeister W
Diabetes Forschungsinstitut, Düsseldorf, F.R.G.
Biomed Biochim Acta. 1991;50(4-6):465-9.
Proteasomes isolated and purified from rat muscle tissue and from the archaebacterium Thermoplasma acidophilum have a very similar size and shape, but the subunit composition is less complex in the archaebacterium as compared to the eukaryotic particle. The archaebacterial enzyme contains a catalytic site with chymotryptic specificity, which is inhibited by serine proteinase inhibitors and clearly differs from the eukaryotic particle which has a minimum of three catalytic sites for peptide bond hydrolysis of a yet undefined mechanism.
从大鼠肌肉组织和嗜热栖热菌古细菌中分离纯化得到的蛋白酶体大小和形状非常相似，但与真核生物颗粒相比，古细菌中的亚基组成没那么复杂。古细菌酶含有一个具有胰凝乳蛋白酶特异性的催化位点，该位点会被丝氨酸蛋白酶抑制剂抑制，且明显不同于真核生物颗粒，后者至少有三个催化位点用于肽键水解，其作用机制尚不明确。
