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rdf:type |
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|
lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1986-9-25
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pubmed:abstractText |
Thyroxine-binding globulin was isolated from pooled human serum by a two-step method involving affinity chromatography on thyroxine-Sepharose and preparative disc-electrophoresis. The final product was found to be homogeneous by polyacrylamide gel electrophoresis and has a molecular weight of 59,000. Isoelectric focusing resolved the protein into seven bands with isoelectric points ranging from 3.9 to 4.3. The isolated protein showed affinity to a number of different dyes as recognized by affinity phase partitioning. The interaction of the protein with the dye Cibacron Blue F3G-A was found to be strongly competitive with the natural ligand thyroxine.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9673
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
6
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|
pubmed:volume |
360
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|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-201
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:3090079-Albumins,
pubmed-meshheading:3090079-Chromatography, Affinity,
pubmed-meshheading:3090079-Coloring Agents,
pubmed-meshheading:3090079-Electrophoresis, Disc,
pubmed-meshheading:3090079-Humans,
pubmed-meshheading:3090079-Hydrogen-Ion Concentration,
pubmed-meshheading:3090079-Isoelectric Focusing,
pubmed-meshheading:3090079-Sodium Chloride,
pubmed-meshheading:3090079-Thyroxine,
pubmed-meshheading:3090079-Thyroxine-Binding Proteins
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pubmed:year |
1986
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|
pubmed:articleTitle |
Partition of purified human thyroxine-binding globulin in aqueous two-phase systems in response to reactive dyes.
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pubmed:publicationType |
Journal Article
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