Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (AtPUMP1) expressed in Escherichia coli.

@article{Borecky2001FunctionalRO,
  title={Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (AtPUMP1) expressed in Escherichia coli.},
  author={Jir{\'i} Borecky and Ivan G Maia and Alexandre Dias Tavares Costa and Petr Je{\vz}ek and Hernan Chaimovich and Paula Milward de Andrade and Anibal E Vercesi and Paulo Henrique Zanella de Arruda},
  journal={FEBS letters},
  year={2001},
  volume={505 2},
  pages={240-4}
}
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… CONTINUE READING
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