The ATPase core of a clathrin uncoating protein.
The ATPase core of a clathrin uncoating protein.
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DOI：
10.1016/s0021-9258(19)75848-7
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发表时间：
1987-01
期刊：
影响因子：
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通讯作者：
T. Chappell;B. Konforti;S. Schmid;J. Rothman
中科院分区：
文献类型：
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作者：
T. Chappell;B. Konforti;S. Schmid;J. Rothman
牛脑脱壳 ATP 酶的胰凝乳蛋白酶消化产生 60 kDa 片段，随后被蛋白水解为 44 kDa。网格蛋白笼脱衣活性的丧失与完整的 70-kDa 酶转化为 60-kDa 片段平行，而网格蛋白结合活性随着 60-kDa 片段降解为 44 kDa 而丧失。该 44 kDa 片段已纯化至均质，并被定性为不依赖于网格蛋白的 ATP 酶。通过使用氨基末端特异性抗体，44-kDa ATP 酶结构域已定位在完整酶内。这种定位与 70 kDa 热休克蛋白家族的保守性有关，牛脑脱壳 ATP 酶是该家族的组成型表达成员。
Chymotryptic digestion of bovine brain uncoating ATPase produced a 60-kDa fragment that was subsequently proteolyzed to 44 kDa. Loss of clathrin cage uncoating activity paralleled the conversion of the intact 70-kDa enzyme to the 60-kDa fragment, while clathrin binding activity was lost as the 60-kDa fragment was degraded to 44 kDa. This 44-kDa fragment has been purified to homogeneity and characterized as a clathrin-independent ATPase. The 44-kDa ATPase domain has been localized within the intact enzyme by the use of amino-terminal specific antibodies. This localization relates to the conserved nature of the 70-kDa heat shock protein family, of which bovine brain uncoating ATPase is a constitutively expressed member.