Linked Life Data

6406104

Source:http://linkedlifedata.com/resource/pubmed/id/6406104

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-7-15
pubmed:abstractText
Thyroxine-binding globulin (TBG) was isolated from pooled whole human serum by diethylaminoethyl (DEAE) Sephadex anion exchange chromatography followed by immunoadsorption chromatography on a cyanogen bromide-activated Sepharose 4B-sheep anti-human TBG immunoadsorbent. Sodium dodecyl sulphate (SDS)-poly-acrylamide gel electrophoresis (PAGE) of the purified TBG revealed a major protein band with a molecular mass of 65 000 and a weak band of molecular mass 54 000 in both reducing and non-reducing buffers. Sedimentation velocity analysis revealed an S20,w coefficient of 4.5S and a calculated molecular mass of 60 000. Immunochemical analysis confirmed the purity of the TBG preparation which gave a single precipitin peak on two-dimensional immunoelectrophoresis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-61
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Isolation of thyroxine-binding globulin (TBG) by immunoadsorption chromatography: some physical and immunochemical characteristics of TBG.
pubmed:publicationType
Journal Article