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Preparation of an ϵ‐deficient chloroplast coupling factor 1 having a high ATPase activity
Author(s) -
Finel Moshe,
Rubinstein Menachem,
Pick Uri
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80050-2
Subject(s) - protein subunit , trypsin , sephadex , atpase , fractionation , chemistry , enzyme , chromatography , biochemistry , chloroform , gamma subunit , extraction (chemistry) , gene
A modification of the chloroform extraction preparation of CF 1 , by elevating the pH during the DEAE‐Sephadex purification step to 7.8 yields a 5‐subunit CF 1 . Different 4‐subunit CF 1 preparations deficient in either δ‐ or ϵ‐subunits, as well as pure β‐subunits are obtained by fractionation of intact CF 1 complex by anion‐exchange high‐performance liquid chromatography. Unlike the 5‐subunit latent enzyme, ϵ‐deficient CF 1 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 CF 1 ‐ATPase activity.