Preparation of an ϵ‐deficient chloroplast coupling factor 1 having a high ATPase activity

FEBS Letters

Rubinstein, Menachem¹  Finel, Moshe²  Pick, Uri² 

[1] Virology Department, The Weizman Institute of Science, Rehovot 76100, Israel;Biochemistry Department, The Weizman Institute of Science, Rehovot 76100, Israel

关键词: Chloroplast coupling factor 1 (CF1);    ATPase regulation;    ϵ-Subunit;    High-performance liquid chromatography;    CF1;    chloroplast coupling factor 1;    DTT;    dithiothreitol;    HPLC;    high-performance liquid chromatography;    OG;    octyl-D-glucopyranoside (octylglucoside);    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(84)80050-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A modification of the chloroform extraction preparation of CF₁, by elevating the pH during the DEAE-Sephadex purification step to 7.8 yields a 5-subunit CF₁. Different 4-subunit CF₁ preparations deficient in either δ- or ϵ-subunits, as well as pure β-subunits are obtained by fractionation of intact CF₁ complex by anion-exchange high-performance liquid chromatography. Unlike the 5-subunit latent enzyme, ϵ-deficient CF₁ has high Ca-ATPase activity which can be inhibited by purified ϵ-subunits. After trypsin or octylglucoside activations all preparations have identical high ATPase activity. These results suggest that the subunit regulates CF₁-ATPase activity.

【 授权许可】

Unknown