Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme.

@article{Yang1987LecithincholesterolAF,
  title={Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme.},
  author={Chao-yuh Yang and Don Manoogian and Q Pao and Frederick S. Lee and Robert H. Knapp and Antonio M. Gotto and Henry J. Pownall},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 7},
  pages={3086-91}
}
The amino acid sequence of human lecithin:cholesterol acyltransferase has been determined by degradation and alignment of peptides obtained from tryptic and staphylococcal digestions and the cleavage with cyanogen bromide and consisted of 416 amino acid residues. All of the tryptic peptides of lecithin:cholesterol acyltransferase were isolated and sequenced. Peptides resulting from digestion by staphylococcal protease, cyanogen bromide cleavage, or the combination of the two methods were… CONTINUE READING

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