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Hydrophobic Protein that Copurifies with Human Brain Acetylcholinesterase
Author(s) -
Navaratnam Dhasakumar S.,
Fernando F. Shama,
Priddle John D.,
Giles Kurt,
Clegg Sheila M.,
Pappin Darryl J.,
Craig Ian,
Smith A. David
Publication year - 2000
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 - 10.1046/j.1471-4159.2000.0742146.x
Subject(s) - acetylcholinesterase , biochemistry , amino acid , gene , peptide sequence , biology , coding region , cysteine , microbiology and biotechnology , sequence analysis , enzyme , chemistry
The mechanism of attachment of acetylcholinesterase (AChE) to neuronal membranes in interneuronal synapses is poorly understood. We have isolated, sequenced, and cloned a hydrophobic protein that copurifies with AChE from human caudate nucleus and that we propose forms a part of a complex of membrane proteins attached to this enzyme. It is a short protein of 136 amino acids and has a molecular mass of 18 kDa. The sequence contains stretches of both hydrophobic and hydrophilic amino acids and two cysteine residues. Analysis of the genomic sequence reveals that the coding region is divided among five short exons. Fluorescence in situ hybridization localizes the gene to chromosome 6p21.32‐p21.2. Northern blot analysis shows that this gene is widely expressed in the brain with an expression pattern that parallels that of AChE.