期刊
FEBS LETTERS
卷 505, 期 2, 页码 240-244出版社
WILEY
DOI: 10.1016/S0014-5793(01)02835-6
关键词
recombinant plant uncoupling protein; reconstitution in liposome; fatty acid-induced proton flux; inhibition by purine nucleotide; Arabidopsis thaliana
The Arabidopsis thaliana uncoupling protein (UCP) gene was expressed in Escherichia coli and isolated protein reconstituted into liposomes. Linoleic acid-induced H+ fluxes were sensitive to purine nucleotide inhibition with an apparent K-i (in mM) of 0.8 (GDP), 0.85 (ATP), 0.98 (GTP), and 1.41 (ADP); the inhibition was pH-dependent. Kinetics of AtPUMP1-mediated H+ fluxes were determined for lauric, myristic, palmitic, oleic, linoleic, and linolenic acids. Properties of recombinant AtPUMP1 indicate that it represents a plant counterpart of animal UCP2 or UCP3. This work brings the functional and genetic approaches together for the first time, providing strong support that AtPUMP1 is truly an UCP. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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