Grinkevich V A, Zaĭtsev V G, Pavlov P F, Nazimov I V, Il'ina E F
Bioorg Khim. 1994 Aug-Sep;20(8-9):842-56.
Unmodified and citraconilated OSCP of the pig heart mitochondrial H(+)-ATPase were hydrolysed by proteinase from Staphylococcus aureus V8 and trypsin, respectively. To purify the individual peptides, various types of HPLC and covalent chromatography on SH-Sepharose were used. By the automatic Edman method complete or partial amino acid sequences of the peptides obtained were determined, thus allowing for the reconstruction of the primary structure of pig OSCP. A linear antigenic determinant recognizable by A1 monoclonal antibody against bovine OSCP, was localized. Studies showed Gly43 residue (bovine OSCP) to be replaced by Ala43 (pig OSCP), which is responsible for a decrease of the affinity of the monoclonal antibody A1 to pig OSCP. Comparative analysis of primary structures of bovine and pig OSCP was carried out.
猪心脏线粒体H(+)-ATP酶的未修饰和柠康酰化的寡霉素敏感性相关蛋白（OSCP）分别被金黄色葡萄球菌V8蛋白酶和胰蛋白酶水解。为了纯化各个肽段，使用了各种类型的高效液相色谱（HPLC）以及在SH-琼脂糖凝胶上的共价色谱法。通过自动埃德曼方法确定了所获得肽段的完整或部分氨基酸序列，从而得以重建猪OSCP的一级结构。定位了一种可被抗牛OSCP的A1单克隆抗体识别的线性抗原决定簇。研究表明，牛OSCP的Gly43残基被猪OSCP的Ala43取代，这导致单克隆抗体A1对猪OSCP的亲和力下降。对牛和猪OSCP的一级结构进行了比较分析。
