Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-4-24
pubmed:abstractText
In the present work we have developed an affinity chromatography system, using haptoglobin bound covalently to Sepharose 4B, to purify hemoglobin from soluble non-heme proteins. Sepharose-haptoglobin specifically binds hemoglobin. It exhibits the same characteristics in its interactions with hemoglobin and alpha or beta hemoglobin chains as does haptoglobin in solution. Globin chains can be eluted from the Sepharose-haptoglobin after removal of the heme. This method has allowed accurate measurements of globin-chain synthesis in blood and bone marrow samples and in culture of early erythroid precursors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
513-9
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Globin-chain affinity chromatography on Sepharose-haptoglobin: a new method of study of hemoglobin synthesis in reticulocytes, in bone marrow and in colonies of erythroid precursors.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't