Crossref journal-article
Wiley
FEBS Letters (311)
Abstract

Isolated chloroplast coupling factor (CF1), when depleted of its ɛ‐subunit, has a high ATPase activity which can be inhibited by binding ɛ to a single high‐affinity (K d = 1.4 × 10−10 M) site. In CF1 reduced by dithiothreitol (DTT), however, ɛ at this binding site is no longer inhibitory. Instead, 3 equivalent, lower affinity (K d = 6 × 10−8 M), inhibitory binding sites for ɛ are observed, whether or not the high‐affinity site contains a bound ɛ‐subunit. Binding of ɛ to the high‐affinity site protects CF1 against trypsin activation, while binding to the low‐affinity site does not, showing that occupation of each class of site has a different effect on CF1 structure. The effects of DTT can be interpreted in terms of a reduction in intersubunit cooperativity in CF1.

Bibliography

Andralojc, P. J., & Harris, D. A. (1988). Two distinct types of ɛ‐binding site exist in chloroplast coupling factor (CF1). FEBS Letters, 233(2), 403–407. Portico.

Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 3:45 a.m.)
Deposited 1 year, 11 months ago (Sept. 16, 2023, 1:29 a.m.)
Indexed 1 year, 11 months ago (Sept. 17, 2023, 12:56 a.m.)
Issued 37 years, 2 months ago (June 20, 1988)
Published 37 years, 2 months ago (June 20, 1988)
Published Online 23 years, 10 months ago (Oct. 19, 2001)
Published Print 37 years, 2 months ago (June 20, 1988)
Funders 0

None

@article{Andralojc_1988, title={Two distinct types of ɛ‐binding site exist in chloroplast coupling factor (CF1)}, volume={233}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(88)80471-x}, DOI={10.1016/0014-5793(88)80471-x}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Andralojc, P.J. and Harris, D.A.}, year={1988}, month=jun, pages={403–407} }