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    
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.
H Heider; U Brodbeck
Related Documents :
3085154 - The demonstration of acetylcholinesterase in plastic sections. its application as a mar...
17335854 - Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner.
1035114 - Kinetics of inhibition of acetylcholinesterase by spin labeled acetylcholine analogs.
7058344 - Hydrolysis of nerve gas by squid-type diisopropyl phosphorofluoridate hydrolyzing enzym...
6445554 - Membrane lipid physical state and modulation of the na+,mg2+-atpase activity in acholep...
3171974 - Use of quinidine inhibition to define the role of the sparteine/debrisoquine cytochrome...
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    
Institut für Biochemie und Molekularbiologie, Universität Bern, Switzerland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Acetylcholinesterase / isolation & purification,  metabolism*
Caudate Nucleus / enzymology*
Centrifugation, Density Gradient
Electrophoresis, Polyacrylamide Gel
Macromolecular Substances
Models, Structural
Molecular Weight
Peptide Fragments / isolation & purification
Polyethylene Glycols
Protein Conformation
Sodium Dodecyl Sulfate / pharmacology
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

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

Previous Document:  Chain-length dependency of interactions of medium-chain fatty acids with glucose metabolism in acini...
Next Document:  Kinetics of the course of inactivation of aminoacylase by 1,10-phenanthroline.