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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1984-4-27
|
| pubmed:abstractText |
A protein with thiamine-binding activity (14 nmole/mg protein) was isolated from rat red cells by affinity chromatography. Adsorbent with varying degrees of hydrophobicity containing thiamine as ligand were used for the isolation. A 2300-fold purification in a 50% overall yield was attained. The purified thiamine-binding protein is homogeneous on polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-8924
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
251-4
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1983
|
| pubmed:articleTitle |
Thiamine-binding protein from rat erythrocytes.
|
| pubmed:publicationType |
Journal Article
|