Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization.

Journal article

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 ...

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Authors: Navaratnam, D; Fernando, F; Priddle, J; Giles, K; Clegg, S

• Publication status: Published
• Journal: Journal of neurochemistry
• Volume: 74
• Issue: 5
• Pages: 2146-2153
• Publication date: 2000-05-01
• DOI: 10.1046/j.1471-4159.2000.0742146.x
• EISSN: 1471-4159
• ISSN: 0022-3042
• Language: English
• Keywords: Amino Acid Sequence; Blotting, Northern; Expressed Sequence Tags; Base Sequence; Molecular Sequence Data; Acetylcholinesterase; Nerve Tissue Proteins; Databases as Topic; Genome; Chromosome Mapping; Humans; Brain