Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.

@article{MacPheeQuigley1985PrimarySO,
  title={Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.},
  author={Kathleen MacPhee-Quigley and Palmer Taylor and Susan S. Taylor},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 22},
  pages={12185-9}
}
Two distinct classes of acetylcholinesterase exist in near equal amounts in the electric organ of Torpedo californica. A globular 5.6 S form is a dimer which possesses a hydrophobic region. The second form is present as elongated species that sediment at 17 and 13 S and contain structural subunits disulfide-linked to the catalytic subunits. Removal of the structural subunits by mild proteolysis yields a tetramer of catalytic subunits which sediments at 11 S. To compare the primary structures of… CONTINUE READING

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