Conformational change of the alpha subunit of Escherichia coli F1 ATPase: ATP changes the trypsin sensitivity of the subunit.
Conformational change of the alpha subunit of Escherichia coli F1 ATPase: ATP changes the trypsin sensitivity of the subunit.
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大肠杆菌F1 ATP酶α亚基的构象变化：ATP改变该亚基的胰蛋白酶敏感性。
DOI：
10.1016/0003-9861(83)90429-0
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发表时间：
1983
影响因子：
3.9
通讯作者：
M. Futai
中科院分区：
文献类型：
--
作者：
M. Senda;H. Kanazawa;T. Tsuchiya;M. Futai
用胰酶研究了大肠杆菌质子转运酶α亚基的构象变化。用少量的胰酶(1μg/mg亚基)将该亚基切割成小于8000dalton的多肽。另一方面，在足够的三磷酸腺苷(1 mM-0.5μm)存在下，亚基被切割成两个主要的多肽(30,000和25,000道尔顿)以饱和亚基的高亲和力位点。亚基与荧光马来酰亚胺结合的酶切分析表明，在核苷酸存在的情况下，亚基在多肽链的中间被消化。ADP和腺苷酰亚胺二磷酸具有与ATP相同的作用。这些结果表明，当ATP与高亲和力结合时，亚基的构象发生了变化，形成了两个胰酶抗性结构域。
Conformational change in the α subunit ofEscherichia coliproton-translocating ATPase was studied using trypsin. The subunit was cleaved with a small amount of trypsin (1 μg/mg subunit) to peptides of less than 8000 daltons. On the other hand, the subunit was cleaved to two main polypeptides (30,000 and 25,000 daltons) in the presence of sufficient ATP (1 mm-0.5 μm) to saturate the high-affinity site of the subunit. Analysis of digests of the subunit combined with fluorescent maleimide suggested that the subunit was digested in the middle of the polypeptide chain in the presence of the nucleotide. ADP and adenylyl imidodiphosphate had the same effect as ATP. These results suggest that the conformation of the subunit changed to form two trypsin-resistant domains upon binding of ATP to the high-affinity site.
ATP 导致大肠杆菌 F1 ATP 酶分离的 α 亚基构象发生巨大变化。
DOI：
--
发表时间：
1980
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Dunn,SD
通讯作者：
Dunn,SD