Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene.

@article{Andresen1996CloningAC,
  title={Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene.},
  author={Brage S Andresen and Peter Bross and Christine Vianey-Saban and Priscille Divry and Marie-Th{\'e}r{\`e}se Zabot and Charles R. Roe and Mohamed A Nada and Anne Grethe Byskov and Torben Arvid Kruse and S\oren Neve and Kurt Kristiansen and Inga Knudsen and Morten Juhl Corydon and N. Gregersen},
  journal={Human molecular genetics},
  year={1996},
  volume={5 4},
  pages={461-72}
}
Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins catalyzing the initial step in fatty acid beta-oxidation. We have used the very fast, Rapid Amplification of cDNA Ends (RACE) based strategy to obtain the sequence of cDNAs encoding human VLCAD from placenta and fibroblasts. Alignment of the predicted amino acid sequence of human VLCAD with those of the other human ACD… CONTINUE READING

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