Document Detail


Monomerization of tetrameric bovine caudate nucleus acetylcholinesterase. Implications for hydrophobic assembly and membrane anchor attachment site.
MedLine Citation:
PMID:  1731764     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Tetrameric detergent-soluble bovine caudate nucleus acetylcholinesterase (AChE) was reduced and alkylated under conditions in which at least 95% of initial activity is retained. This treatment alone did not result in monomerization of AChE, nor did it create a hydrophilic enzyme. However, in the presence of SDS the enzyme became monomerized. Incubation of AChE with trypsin in the presence of the reversible inhibitor edrophonium rendered the enzyme hydrophilic and led to catalytically active monomers being produced. SDS/PAGE of this preparation in non-reducing conditions revealed only a small decrease in the subunit molecular mass. N-Terminal sequencing of the enzyme, before and after trypsin treatment, yielded identical N-termini showing that the enzyme was monomerized subsequent to C-terminal tryptic cleavage. From our results, we conclude that the most C-terminal cysteine residue is involved in inter-subunit disulphide bonding as well as in the attachment of AChE to the membrane anchor. Furthermore, the C-terminal region in the primary structure provides an area for hydrophobic contacts between the different subunits and also between the subunits and the membrane anchor.
Authors:
H Heider; U Brodbeck
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  281 ( Pt 1)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1992 Jan 
Date Detail:
Created Date:  1992-02-18     Completed Date:  1992-02-18     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  279-84     Citation Subset:  IM    
Affiliation:
Institut für Biochemie und Molekularbiologie, Universität Bern, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Acetylcholinesterase / isolation & purification,  metabolism*
Animals
Cattle
Caudate Nucleus / enzymology*
Centrifugation, Density Gradient
Detergents
Electrophoresis, Polyacrylamide Gel
Macromolecular Substances
Models, Structural
Molecular Weight
Octoxynol
Peptide Fragments / isolation & purification
Polyethylene Glycols
Protein Conformation
Sodium Dodecyl Sulfate / pharmacology
Chemical
Reg. No./Substance:
0/Detergents; 0/Macromolecular Substances; 0/Peptide Fragments; 0/Polyethylene Glycols; 151-21-3/Sodium Dodecyl Sulfate; 9002-93-1/Octoxynol; EC 3.1.1.7/Acetylcholinesterase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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