Molecular structures of acetylcholinesterase from electric organ tissue of the electric eel

Proc Natl Acad Sci U S A. 1973 Sep;70(9):2473-6. doi: 10.1073/pnas.70.9.2473.

Abstract

Three purified molecular forms of acetylcholinesterase (EC 3.1.1.7) with sedimentation coefficients of 18 S, 14 S, and 11 S were studied by analytical ultracentrifugation and electron microscopy. The three species have molecular weights of (1.1 +/- 0.1) x 10(6), (7.5 +/- 1.5) x 10(5), and (3.35 +/- 0.25) x 10(5), respectively. Electron micrographs reveal that the 18S and 14S forms are asymmetric, composed of a head, containing a large number of subunits, and an elongated tail. The 11S form of acetylcholinesterase is apparently a tetrameric structure devoid of the tail. Maleylation of 18S and 14S acetylcholinesterases abolishes their tendency to aggregate at low ionic strength.

MeSH terms

  • Acetylcholinesterase*
  • Animals
  • Centrifugation, Density Gradient
  • Eels
  • Electric Organ / enzymology*
  • Maleates
  • Microscopy, Electron
  • Molecular Conformation
  • Molecular Weight

Substances

  • Maleates
  • Acetylcholinesterase