Document Detail


VAT-1 from Torpedo electric organ forms a high-molecular-mass protein complex within the synaptic vesicle membrane.
MedLine Citation:
PMID:  8365405     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
VAT-1 is an abundant 41-kDa protein from Torpedo cholinergic synaptic vesicles. Most of VAT-1 immunoreactivity (70%) is localized to the synaptic vesicle membrane while the rest (30%) copurifies with larger membranous fragments. VAT-1 forms a high-molecular-mass complex within the synaptic vesicle membrane. The Stokes radius of the VAT-1 complex is 4.85 nm and the sedimentation coefficient is 8.0 x 10(-13) S. Using these values, the calculated apparent mass of the VAT-1 complex is 176 kDa and the friction coefficient is consistent with that for a globular protein. Electrophoresis of solubilized synaptic vesicle proteins following cross-linking resulted in a 40-kDa ladder which was detected by VAT-1 antibodies. This is in accord with VAT-1 protein complex being composed primarily of VAT-1 subunits. The hydrodynamic characteristics of the VAT-1 protein complex suggest that it is composed of three or four VAT-1 subunits. Synaptophysin, an abundant component of Torpedo synaptic vesicle membranes, which has a similar apparent size as VAT-1, is not part of the VAT-1 protein complex. Interactions between the subunits within the protein complex do not depend on disulfide bonds or on lowering the ionic strength. However, partial dissociation of VAT-1 subunits from the complex occurs by chelating calcium ions.
Authors:
M Linial
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  216     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1993 Aug 
Date Detail:
Created Date:  1993-10-07     Completed Date:  1993-10-07     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  189-97     Citation Subset:  IM    
Affiliation:
Department of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium / metabolism
Chromatography, Gel
Disulfides
Electric Organ / chemistry
Immunoblotting
Membrane Proteins / analysis,  chemistry,  metabolism*
Molecular Weight
Nerve Tissue Proteins / analysis,  chemistry,  metabolism*
Silver Staining
Synaptic Vesicles / chemistry,  metabolism*
Synaptophysin / analysis,  chemistry
Torpedo
Chemical
Reg. No./Substance:
0/Disulfides; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Synaptophysin; 0/VAT-1 protein, Torpedo; 7440-70-2/Calcium

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