pubmed-article:8738328 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0025552 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0034303 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0038128 | lld:lifeskim |
pubmed-article:8738328 | lifeskim:mentions | umls-concept:C0183683 | lld:lifeskim |
pubmed-article:8738328 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8738328 | pubmed:dateCreated | 1997-2-7 | lld:pubmed |
pubmed-article:8738328 | 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. | lld:pubmed |
pubmed-article:8738328 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:language | eng | lld:pubmed |
pubmed-article:8738328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8738328 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8738328 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8738328 | pubmed:issn | 0173-0835 | lld:pubmed |
pubmed-article:8738328 | pubmed:author | pubmed-author:SheproDD | lld:pubmed |
pubmed-article:8738328 | pubmed:author | pubmed-author:GaoJ HJH | lld:pubmed |
pubmed-article:8738328 | pubmed:author | pubmed-author:PattonW FWF | lld:pubmed |
pubmed-article:8738328 | pubmed:author | pubmed-author:ShojaeeNN | lld:pubmed |
pubmed-article:8738328 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8738328 | pubmed:volume | 17 | lld:pubmed |
pubmed-article:8738328 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8738328 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8738328 | pubmed:pagination | 687-93 | lld:pubmed |
pubmed-article:8738328 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8738328 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8738328 | pubmed:articleTitle | Pyrogallol red-molybdate: a reversible, metal chelate stain for detection of proteins immobilized on membrane supports. | lld:pubmed |
pubmed-article:8738328 | pubmed:affiliation | Microvascular Research Laboratory, Boston University, MA 02215, USA. | lld:pubmed |
pubmed-article:8738328 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8738328 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8738328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |