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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1983-12-20
|
| pubmed:abstractText |
The association constant for binding of vitamin B12 (cyanocobalamin) by human intrinsic factor coupled to Sepharose 4B and the concentration of binding sites of the coupled intrinsic factor have been measured as a function of pH, temperature, ionic strength and the presence of various (ionic and non-ionic) components in the solution.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0020-708X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
34
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1351-6
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading | |
| pubmed:year |
1983
|
| pubmed:articleTitle |
The influence of experimental conditions on the association constant for binding of vitamin B12 by human intrinsic factor coupled to Sepharose 4B.
|
| pubmed:publicationType |
Journal Article
|