ε-Binding regions of the γ subunit of Escherichia coli ATP synthase
ε-Binding regions of the γ subunit of Escherichia coli ATP synthase
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大肠杆菌 ATP 合酶 γ 亚基的 ε-结合区域
DOI：
10.1016/s0005-2728(96)00159-4
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
S. Dunn
中科院分区：
文献类型：
--
作者：
S. Dunn
本文用单克隆抗体和~（125）I-ε配体印迹法研究了大肠杆菌ATP合成酶F_1-ATP酶γ亚基和ε亚基之间的相互作用。单克隆抗体（MAb）γ-1能与ε缺失的F1-ATPase结合，但不能与ε充实的F1结合，表明ε阻断了对表位的接近。建立了125 I-ε与γ结合的配体印迹法。单克隆抗体γ-1和第二种抗体（单克隆抗体γ Ⅱ）均能抑制~（125）I-ε与γ的结合，而另外两种抗γ单克隆抗体则不能。MAb γ-1识别的抗原表位位于R49和R70残基之间，与MAb γII的抗原表位相距甚远，后者位于286个氨基酸残基多肽的K199残基的C端。这些抗体与ε竞争结合γ意味着它们的表位在序列上完全分开，都位于参与结合ε的亚基的部分。
The interaction between the γ and ε subunits of the F1-ATPase sector of Escherichia coli ATP synthase has been investigated using monoclonal antibodies directed against the γ subunit and ligand blotting using125I-ε. Monoclonal antibody (MAb) γ-1 was able to bind to ε-depleted F1-ATPase but not to ε-replete F1, implying that ε blocked access to the epitope. A ligand blot assay for the binding of125I-ε to γ was developed. Both MAb γ-1 and a second antibody, MAb γII, inhibited binding of125I-ε to γ in this assay while two other anti-γ monoclonal antibodies did not. The epitope recognized by MAb γ-1 was mapped between residues R49 and R70, quite distant in sequence from that of MAb γII, which is located C-terminal to residue K199 of the 286-residue polypeptide. The competition of these antibodies with ε for binding to γ implies that their epitopes, quite separate in sequence, are both located in parts of the subunit involved in binding ε.
DOI：
10.1093/protein/1.1.67
发表时间：
1986-10-01
期刊：
PROTEIN ENGINEERING
影响因子：
--
作者：
MEAD, DA;SZCZESNASKORUPA, E;KEMPER, B
通讯作者：
KEMPER, B
大肠杆菌腺苷三磷酸酶中ε亚基构象的催化位点核苷酸和无机磷酸盐依赖性。
影响因子：
2.9
作者：
Mendel-Hartvig,J;Capaldi,RA
通讯作者：
Capaldi,RA
DOI：
10.1073/pnas.92.24.10964
发表时间：
1995-11-21
影响因子：
11.1
作者：
DUNCAN, TM;BULYGIN, VV;CROSS, RL
通讯作者：
CROSS, RL