Abstract:
: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.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Navaratnam DS,Fernando FS,Priddle JD,Giles K,Clegg SM,Pappin DJ,Craig I,Smith ADdoi
10.1046/j.1471-4159.2000.0742146.xkeywords:
subject
Has Abstractpub_date
2000-05-01 00:00:00pages
2146-53issue
5eissn
0022-3042issn
1471-4159journal_volume
74pub_type
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