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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.

Type

Journal article

Journal

J Neurochem

Publication Date

05/2000

Volume

74

Pages

2146 - 2153

Keywords

Acetylcholinesterase, Amino Acid Sequence, Base Sequence, Blotting, Northern, Brain, Chromosome Mapping, Databases as Topic, Expressed Sequence Tags, Genome, Humans, Molecular Sequence Data, Nerve Tissue Proteins