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Heterogeneity of Rat Brain Acetylcholinesterase: A Study by Gel Filtration and Gradient Centrifugation
Author(s) -
Rakonczay Z.,
Vincendon G.,
Zanetta JP.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb12538.x
Subject(s) - acetylcholinesterase , filtration (mathematics) , centrifugation , size exclusion chromatography , chromatography , differential centrifugation , chemistry , biochemistry , enzyme , mathematics , statistics
According to their solubilization properties, two classes of acetyl‐cholinesterases (AChE) can be detected in the adult rat brain: a “soluble” species (easily solubilized without detergent), and a membrane‐bound species (solubilized only in the presence of detergent). The latter was found to be homogeneous by gel filtration (Stokes radius 8.05 ± 0.35 nm) and sucrose gradient centrifugation (9.75 ± 0.2 S) in the presence of Triton X‐100. The “soluble” AChE gives three stable species in the presence of the same detergent with Stokes radii and sedimentation constants of 10.9 ± 0.5 nm and 16 ± 2 S; 6.75 ± 0.30 nm and 10.7 ± 0.4 S; 5.37 ± 0.35 nm and 4.37 ± 0.1 S. Co‐chromatography and co‐sedimentation or the reduction and alkylation of disulfide bridges show that all the soluble species are different from the membrane‐bound AChE. The possibility that soluble and membrane‐bound AChE are completely different molecules is discussed.