An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity.

@article{Siloto2008AnNF,
  title={An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity.},
  author={Rodrigo M. P. Siloto and Milan Madhavji and William B Wiehler and Tracy L Burton and Parveen S Boora and Andr{\'e} Laroche and Randall J Weselake},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={373 3},
  pages={350-4}
}
A histidine-tagged recombinant N-terminal fragment of type-1 mouse liver diacylglycerol acyltransferase (DGAT; EC 2.3.1.20), MmDGAT1(1-95)His6, was expressed in Escherichia coli, and used to investigate possible acyl-CoA-binding properties. Analysis of the purified fragment by MALDI-TOF mass spectrometry revealed a polypeptide with molecular mass of about 11 kDa which was consistent with the calculated molecular mass based on the deduced amino acid sequence. Lipidex-1000 binding assays… CONTINUE READING