Paper Report for: Saez-Valero_1993_J.Neurosci.Res_35_678
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Title: Amphiphilic and hydrophilic forms of acetyl- and butyrylcholinesterase in human brain Saez-Valero J, Tornel PL, Munoz-Delgado E, Vidal CJ Ref: Journal of Neuroscience Research, 35:678, 1993 : PubMed
Human brain acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) were sequentially extracted, first with a Tris-saline buffer (S1) and then with 1% (w/v) Triton X-100 (S2). About 20 and 30% of the AChE and BCHE activities were recovered in S1 and most of the remaining enzymes in S2. Main molecular forms of about 10.5 S and 12.0 S, G4 forms of AChE and BCHE, and smaller amounts of 4.5 S and 5.5 S forms, G1 species of AChE and BCHE, were measured in S1. Application of Triton X-114 phase partitioning and affinity chromatography on phenyl-agarose to S1 revealed that 25% of the AChE and none of the BCHE molecules displayed amphiphilic properties. Analysis of the enzyme activity retained by the phenyl-agarose showed that G1 AChE constituted the bulk of the amphiphilic molecules released without detergent. Main G4 forms of AChE and BCHE were found in the S2 extract. Eighty and 45% of the AChE and BCHE activities in S2 were measured in the detergent-rich phase by Triton X-114 phase partitioning. Thus, most of the AChE and about half of the BCHE molecules in S2 displayed amphiphilic properties. The main peak of BCHE, a 12.0 S form in gradients made with Triton X-100, splits into two peaks of 9.5 S and 12.5 S in Brij 96-containing gradients. This suggests that hydrophilic G4 BCHE forms are predominant in S1 and that hydrophilic and amphiphilic isoforms coexist in S2.
        
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Saez-Valero J, Tornel PL, Munoz-Delgado E, Vidal CJ (1993) Amphiphilic and hydrophilic forms of acetyl- and butyrylcholinesterase in human brain Journal of Neuroscience Research35: 678-89
Saez-Valero J, Tornel PL, Munoz-Delgado E, Vidal CJ (1993) Journal of Neuroscience Research35: 678-89