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By L. A. Greene, J. M. Aletta, D. E. Burstein, S. A. Drexler (auth.), Professor Dr. Bernd Hamprecht, Professor Dr. Volker Neuhoff (eds.)

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Biochim Biophys Acta 657:243-256 Robinson NC, Tanford C (1975) The binding of deoxycholate, Triton X-I00, sodium dodecyl sulfate and phosphatidylcholine vesicles to cytochrome b5. Biochemistry 14:369-378 Romer-Luthi CR, Ott P, Brodbeck U (1980) Reconstitution of human erythrocyte membrane acetylcholinesterase in phospholipid vesicles. Analysis of the molecular forms by cross-linking studies. Biochim Biophys Acta 601:123-133 Rosenberry TL, Scoggin DM (1984) Structure of human erythrocyte acetylcholinesterase.

In: Brzin M, Barnard EA, Sket D (eds) Cholinesterases: Fundamental and applied aspects. De Gruyter, Berlin, pp 155-172 Rosenbusch JP, Garavito RM, Dorset DL, Engel A (1982) Structure and Function of a pore-forming transmembrane protein: high resolution studies of a bacterial porin. In: Peters H (ed) Protides of the biological fluids. colloq 29. Pergamon Press, Oxford, pp 171-174 Rotundo RL (1984) Purification and properties of the membrane-bound form of acetylcholinesterase from chicken brain. J BioI Chem 259:13189-13194 Ruess KP, Lieflander M (1981) Molecular forms of purified cytoplasmatic and membrane bound bovine-brain-acetylcholinesterase solubilized by different methods.

1984), the 04 enzyme from bovine brain contains only two active sites per tetramer, and they suggested that this form consists of pairs of dislike subunits. SOS-polyacrylamide gel electrophoresis in nonreducing conditions of form 04 from human brain also showed two pairs of subunits appearing at 150,000 and 130,000 daltons (Gennari and Brodbeck 1985). The functional molarity of this enzyme, however, was determined as four active sites per tetramer (Gentinetta and Brodbeck, unpublished). The molecular weights obtained in nonreducing conditions are in all forms of OS-AChE about twice that obtained in reducing conditions, which suggests that pairs of subunits are interlinked by disulfide bridges.

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