Characterization of the Acyl-CoA synthetase activity of purified murine fatty acid transport protein 1.

@article{Hall2003CharacterizationOT,
  title={Characterization of the Acyl-CoA synthetase activity of purified murine fatty acid transport protein 1.},
  author={Angela M. Hall and Anne K. Smith and David A Bernlohr},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 44},
  pages={43008-13}
}
Fatty acid transport protein 1 (FATP1) is an approximately 63-kDa plasma membrane protein that facilitates the influx of fatty acids into adipocytes as well as skeletal and cardiac myocytes. Previous studies with FATP1 expressed in COS1 cell extracts suggested that FATP1 exhibits very long chain acyl-CoA synthetase (ACS) activity and that such activity may be linked to fatty acid transport. To address the enzymatic activity of the isolated protein, murine FATP1 and ACS1 were engineered to… CONTINUE READING

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  • H. Irie, I. B. Krukenkamp, +6 authors A. Ibrahimi
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