Zakharov S D, Sytnik S K, Mal'yan A N, Makarov A D
Biokhimiia. 1978 May;43(5):887-91.
An isolation procedure is worked out and properties are studied of CF1 ATPase from chloroplasts with changed submolecular structure. The enzyme, isolated by chlorophorm treatment, produced Ca-dependent ATPase activity in water solution. As compared with the enzyme isolated by well known Lien and Racker method, the enzyme preparation obtained is slightly activated by heating, is not activated by trypsin and has a lesser ability to recover ATP synthesis in EDTA-treated chloroplasts. Purification on DEAE-Sephadex produced the enzyme preparation free of delta-subunit. Chlorophorm treatment is suggested to change submolecular protein structure, in particular, loosening of the link of delta-subunit with other enzyme subunits. The data obtained suggest that delta-subunit participates in the binding of CF1 ATPase with chloroplast membrane.
制定了一种分离程序，并对亚分子结构发生变化的叶绿体CF1 ATP酶的性质进行了研究。通过氯仿处理分离得到的这种酶，在水溶液中产生了依赖于钙的ATP酶活性。与通过著名的利恩和拉克尔方法分离得到的酶相比，所获得的酶制剂经加热后略有激活，不被胰蛋白酶激活，并且在经乙二胺四乙酸（EDTA）处理的叶绿体中恢复ATP合成的能力较弱。在二乙氨基乙基葡聚糖（DEAE - Sephadex）上进行纯化得到了不含δ亚基的酶制剂。有人提出氯仿处理会改变亚分子蛋白质结构，特别是δ亚基与其他酶亚基之间连接的松弛。所获得的数据表明，δ亚基参与CF1 ATP酶与叶绿体膜的结合。
