| Characterization of a tetrameric G4 form of acetylcholinesterase from bovine brain: a comparison with the dimeric G2 form of the electric organ. | |
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MedLine Citation:
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PMID: 3173345 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Globular forms (G forms) of acetylcholinesterase (AChE) are formed by monomers, dimers and tetramers of the catalytic subunits (G1, G2 and G4). In this work the hydrophobic G2 and G4 AChE forms were purified to homogeneity from Discopyge electric organ and bovine caudate nucleus and studied from different points of view, including: velocity sedimentation, affinity to lectins and SDS-polyacrylamide gel electrophoresis under reducing and non-reducing conditions. The polypeptide composition of Discopyge electric organ G2 is similar to Torpedo, however the pattern of the brain G4 AChE is much complex. Under non-reducing conditions the catalytic subunit possesses a molecular weight of 65 kDa, however this value increases to 68 kDa after reduction, suggesting that intrachain-disulfide bonds are important in the folding of the catalytic subunits of the AChE. Also it was found that after mild proteolysis; the (125I)-TID-20 kDa fragment decreased its molecular weight to approximately 10 kDa with little loss of AChE activity. Finally, we suggest a model for the organization of the different domains of the hydrophobic anchor fragment of the G4 form. |
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Authors:
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M E Fuentes; N C Inestrosa |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular and cellular biochemistry Volume: 81 ISSN: 0300-8177 ISO Abbreviation: Mol. Cell. Biochem. Publication Date: 1988 May |
Date Detail:
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Created Date: 1988-11-21 Completed Date: 1988-11-21 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0364456 Medline TA: Mol Cell Biochem Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 53-64 Citation Subset: IM |
Affiliation:
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Department of Cell Biology, Faculty of Biological Sciences, Catholic University of Chile, Santiago. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acetylcholinesterase
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analysis*,
isolation & purification Animals Brain / enzymology* Cattle Centrifugation, Density Gradient Electric Fish* Electric Organ / enzymology* Electrophoresis, Polyacrylamide Gel Endopeptidase K Lectins / metabolism Serine Endopeptidases / metabolism Solubility Temperature Wheat Germ Agglutinins |
| Chemical | |
Reg. No./Substance:
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0/Lectins; 0/Wheat Germ Agglutinins; EC 3.1.1.7/Acetylcholinesterase; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.64/Endopeptidase K |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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