Molnar E, Varga S, Jona I, Seidler N W, Martonosi A
Department of Biochemistry and Molecular Biology, State University of New York, Syracuse 13210.
Biochim Biophys Acta. 1992 Jan 31;1103(2):281-95. doi: 10.1016/0005-2736(92)90098-7.
The effect of anti-ATPase antibodies with epitopes near Asp-351 (PR-8), Lys-515 (PR-11) and the ATP binding domain (D12) of the Ca(2+)-ATPase of sarcoplasmic reticulum (EC 3.6.1.38) was analyzed. The PR-8 and D12 antibodies reacted freely with the Ca(2+)-ATPase in the native membrane, indicating that their epitopes are exposed on the cytoplasmic surface. Both PR-8 and D12 interfered with the crystallization of the Ca(2+)-ATPase, suggesting that their binding sites are at interfaces between ATPase molecules. PR-11 had no effect on ATPase-ATPase interactions or on the ATPase activity of sarcoplasmic reticulum. The epitope of PR-11 is suggested to be the VIDRC sequence at residues 520-525, while that of D12 at residues 670-720 of the Ca(2+)-ATPase. The use of predictive algorithms of antigenicity for identification of potential antigenic determinants in the Ca(2+)-ATPase is analyzed.
分析了抗ATP酶抗体对肌浆网（EC 3.6.1.38）Ca(2 +)-ATP酶中靠近天冬氨酸-351（PR - 8）、赖氨酸-515（PR - 11）的表位以及ATP结合域（D12）的影响。PR - 8和D12抗体能与天然膜中的Ca(2 +)-ATP酶自由反应，这表明它们的表位暴露于细胞质表面。PR - 8和D12均干扰了Ca(2 +)-ATP酶的结晶，提示它们的结合位点位于ATP酶分子之间的界面处。PR - 11对ATP酶-ATP酶相互作用或肌浆网的ATP酶活性没有影响。PR - 11的表位推测为Ca(2 +)-ATP酶520 - 525位残基处的VIDRC序列，而D12的表位位于Ca(2 +)-ATP酶670 - 720位残基处。分析了使用抗原性预测算法来鉴定Ca(2 +)-ATP酶中潜在抗原决定簇的情况。
