| VAT-1 from Torpedo electric organ forms a high-molecular-mass protein complex within the synaptic vesicle membrane. | |
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MedLine Citation:
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PMID: 8365405 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M Linial |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 216 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1993 Aug |
Date Detail:
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Created Date: 1993-10-07 Completed Date: 1993-10-07 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 189-97 Citation Subset: IM |
Affiliation:
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Department of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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0/Disulfides; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Synaptophysin; 0/VAT-1 protein, Torpedo; 7440-70-2/Calcium |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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