IN-VITRO ACTIVATION OF THE 20S PROTEASOME
IN-VITRO ACTIVATION OF THE 20S PROTEASOME
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DOI：
10.1159/000468685
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发表时间：
1993-01-01
期刊：
影响因子：
--
通讯作者：
KUEHN, L
中科院分区：
文献类型：
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作者：
DAHLMANN, B;BECHER, B;KUEHN, L
研究了十二烷基硫酸钠、甘油脂肪酸酯、肉碱和辅酶A、磷脂、组蛋白、多聚赖氨酸等化合物以及同双功能化学交联剂对哺乳动物蛋白酶体各种蛋白分解活性的影响。大多数试剂增强了这些活性，一些试剂，如脂肪酸辅酶A酯、组蛋白和化学交联剂，根据所测量的活性，产生双重作用，即同时激活和抑制。在适宜的十二烷基硫酸钠激活浓度下，电子显微镜不能检测到蛋白酶体的结构变化。在超最佳洗涤剂浓度下形成胶束可能是蛋白酶体不可逆变性的一个原因。
The effect of chemical compounds like sodium dodecyl sulfate (SDS), fatty acid esters of glycerol, carnitine and coenzyme A, phospholipids, histones, polylysines as well as homobifunctional chemical cross-linkers on the various proteolytic activities of mammalian proteasomes have been tested. Most of the reagents enhance these activities, and some, e.g. fatty acid CoA esters, histones and the chemical cross-linkers, exert dual effects, i.e. activation and inhibition at the same time, depending on the activity measured. With optimally activating concentrations of SDS, no structural changes in proteasomes can be detected by electron microscopy. Formation of micelles at supra-optimal detergent concentrations may be a reason for irreversible denaturation of the proteasome.