Linked Life Data

7199356

Source:http://linkedlifedata.com/resource/pubmed/id/7199356

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-5-21
pubmed:abstractText
A protein with binding specificity for retinol was purified from human liver. [3H]Retinol was added to liver extracts and the [3H]retinol-binding protein isolated by conventional chromatographic techniques including ion-exchange chromatography on DEAE-Sepharose, gel filtration on Sephadex G-75 and G-50 and preparative isoelectric focusing. The yield was 10-15% in different preparations and the degree of purification was about 3000-fold. The purified protein had a molecular weight of about 15,000 as estimated from both gel filtration and polyacrylamide gel electrophoresis in sodium dodecyl sulphate and homogeneous in several electrophoretic systems. Isoelectric focusing of the purified protein gave a doublet band. Only one fluorescent band at pH 4.70 was seen if the protein solution was incubated with excess retinol prior to isoelectric focusing. The isolated protein did not react with antiserum to the retinol-binding protein of plasma. The amino acid composition and the amino terminal amino acid sequence for the first sixteen amino acids of the purified protein differed significantly from that of the plasma retinol-binding protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
714
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
536-42
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and partial characterization of a cellular retinol-binding protein from human liver.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't