| Isolation and characterization of beta-gliadin fractions. | |
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MedLine Citation:
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PMID: 7417494 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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beta-Gliadins of Cappelle wheat are distributed in three subsets in starch gel electrophoresis at pH 3.2, Six of these beta components have been isolated by sulfopropyl-Sephadex C-50 chromatography, gel filtration on Sephadex G-100 and sulfoethyl-cellulose chromatography. Apparent molecular weights determined by gel filtration and SDS-polyacrylamide gradient gel electrophoresis are between 29 000 and 35 000. Valine is the N-terminal amino acid of all beta-gliadins with the exception of the slowest component in electrophoresis at pH 3.2 the N-terminal amino acid of which is asparagine. The main difference between the amino acid compositions is the lack of tryptophan in the fastest of the three component subsets visible in electrophoresis at pH 3.2. |
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Authors:
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T Tercé-Laforgue; L Charbonnier; J Mossé |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 625 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1980 Sep |
Date Detail:
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Created Date: 1980-12-16 Completed Date: 1980-12-16 Revised Date: 2002-11-01 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 118-26 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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analysis Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Gliadin / analysis*, isolation & purification Hydrogen-Ion Concentration Molecular Weight Plant Proteins / analysis* Triticum |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Plant Proteins; 9007-90-3/Gliadin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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