Complete cDNA encoding human phospholipid transfer protein from human endothelial cells.

@article{Day1994CompleteCE,
  title={Complete cDNA encoding human phospholipid transfer protein from human endothelial cells.},
  author={Joseph R Day and John J. Albers and Catherine E. Lofton-Day and Tari L Gilbert and Andrew T. Ching and F. J. Grant and P. J. O'Hara and Santica M. Marcovina and Janet L. Adolphson},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 12},
  pages={9388-91}
}
Phospholipid transfer protein, with an apparent molecular mass of 81 kDa, was purified from human plasma. The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full-length cDNA from a human endothelial cDNA library. The cDNA is 1,750 base pairs in length and contains an open reading frame of 1,518 nucleotides encoding a leader of 17… CONTINUE READING

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The cDNA is 1,750 base pairs in length and contains an open reading frame of 1,518 nucleotides encoding a leader of 17 amino acids and a mature protein of 476 residues .
The cDNA is 1,750 base pairs in length and contains an open reading frame of 1,518 nucleotides encoding a leader of 17 amino acids and a mature protein of 476 residues .
The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full - length cDNA from a human endothelial cDNA library .
The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full - length cDNA from a human endothelial cDNA library .
The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full - length cDNA from a human endothelial cDNA library .
The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full - length cDNA from a human endothelial cDNA library .
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