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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1997-2-7
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pubmed:abstractText |
Certain metal complexes selectively interact with proteins immobilized on solid-phase membrane supports to form brightly colored products. The metal chelates form protein-dye complexes in the presence of metal ions at acidic pH but are eluted from the proteins by immersing membranes in a solution of basic pH that contains other chelating agents. The reversible nature of the protein staining procedure allows for subsequent biochemical analyses, such as immunoblotting, N-terminal and internal protein sequencing. Among the metal complexes evaluated to date, the triazine dye-ferrous complexes (ferene S, ferrozine) and the ferrocyanide-ferric complexes provide the most sensitive detection of proteins immobilized on membranes. While the pyrogallol red-molybdate complex is commonly used in solution-based total protein assays, its utility as a reversible stain for proteins immobilized on membranes has not been reported. Pyrogallol red-molybdate complexes readily stain proteins on nitrocellulose and polyvinyl difluoride membranes with similar sensitivity as ferrozine-ferrous complexes. Analysis of charge-fractionated carrier ampholytes and synthetic polymers of different L-amino acids indicate that binding is prominently via protonated alpha and epsilon-amino side chains. Carbamylation of amino groups in bovine serum albumin substantially diminishes pyrogallol red-molybdate binding to the protein. The stain is reversible, resistant to chemical interference, and compatible with immunoblotting.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Collodion,
http://linkedlifedata.com/resource/pubmed/chemical/Coloring Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Membranes, Artificial,
http://linkedlifedata.com/resource/pubmed/chemical/Molybdenum,
http://linkedlifedata.com/resource/pubmed/chemical/Polyvinyls,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrogallol,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/polyvinylidene fluoride,
http://linkedlifedata.com/resource/pubmed/chemical/pyrogallol sulfonphthalein,
http://linkedlifedata.com/resource/pubmed/chemical/sodium molybdate(VI)
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0173-0835
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
687-93
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8738328-Chelating Agents,
pubmed-meshheading:8738328-Collodion,
pubmed-meshheading:8738328-Coloring Agents,
pubmed-meshheading:8738328-Immunoblotting,
pubmed-meshheading:8738328-Membranes, Artificial,
pubmed-meshheading:8738328-Molecular Structure,
pubmed-meshheading:8738328-Molybdenum,
pubmed-meshheading:8738328-Polyvinyls,
pubmed-meshheading:8738328-Pyrogallol,
pubmed-meshheading:8738328-Sensitivity and Specificity,
pubmed-meshheading:8738328-Serum Albumin, Bovine
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pubmed:year |
1996
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pubmed:articleTitle |
Pyrogallol red-molybdate: a reversible, metal chelate stain for detection of proteins immobilized on membrane supports.
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pubmed:affiliation |
Microvascular Research Laboratory, Boston University, MA 02215, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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