Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C.

A dimeric form of acetylcholinesterase from Torpedo californica was purified to homogeneity by affinity chromatography subsequent to solubilization with a phosphatidylinositol-specific phospholipase C of bacterial origin. Bipyramidal crystals of the enzyme were obtained from solutions in polyethylene glycol 200. The crystals diffract to 2.0 A (1 A = 0.1 nm) resolution. They were found to be orthorhombic, space group P2221, with a = 163.4(+/- 0.2) A, b = 112.1(+/- 0.2) A, c = 81.3(+/- 0.1) A.

[1]  G. G. Stokes.  "J." , 1890, The New Yale Book of Quotations.

[2]  B. Hasinoff.  Kinetics of acetylthiocholine binding to electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity. Evidence for a diffusion-controlled reaction. , 1982, Biochimica et biophysica acta.

[3]  M. Ferguson,et al.  Covalently attached phosphatidylinositol as a hydrophobic anchor for membrane proteins , 1986 .

[4]  I. Silman,et al.  Molecular structure of elongated forms of electric eel acetylcholinesterase. , 1978, Journal of molecular biology.

[5]  Y. Dudai,et al.  Purification by affinity chromatography of acetylcholinesterase from electric organ tissue of the electric eel subsequent to tryptic treatment. , 1972, Biochimica et biophysica acta.

[6]  S. Taylor,et al.  Profile of the disulfide bonds in acetylcholinesterase. , 1986, The Journal of biological chemistry.

[7]  I. Silman,et al.  A hydrophobic dimer of acetylcholinesterase from Torpedo californica electric organ is solubilized by phosphatidylinositol-specific phospholipase C , 1983, Neuroscience Letters.

[8]  S. Taylor,et al.  Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences. , 1985, The Journal of biological chemistry.

[9]  Susan S. Taylor,et al.  Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence , 1986, Nature.

[10]  I Silman,et al.  Identification of covalently bound inositol in the hydrophobic membrane-anchoring domain of Torpedo acetylcholinesterase. , 1985, Biochemical and biophysical research communications.

[11]  G. Koelle.  Cholinesterases and Anticholinesterase Agents , 1963 .

[12]  F. Rieger,et al.  Solubilisation de l'acétylcholinestérase des organes électriques de gymnote , 1970 .

[13]  C. Chothia,et al.  Acetylcholinesterase: the structure of crystals of a globular form from electric eel. , 1975, Journal of molecular biology.

[14]  I. Wilson,et al.  Acetylcholinesterase — the acyl-enzyme intermediate , 1980, Neurochemistry International.

[15]  I. Silman,et al.  Modes of attachment of acetylcholinesterase to the surface membrane. , 1987, European journal of biochemistry.

[16]  B. Matthews.  Solvent content of protein crystals. , 1968, Journal of molecular biology.