Linked Life Data

1400505

Source:http://linkedlifedata.com/resource/pubmed/id/1400505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1992-11-25
pubmed:abstractText
Polyclonal antibodies were raised against the nitrobenzylthioinosine (NBMPR)-sensitive nucleoside transporter of human erythrocyte membranes. On Western blots of these membranes they labeled the broad "band 4.5" region (average apparent M(r) 55,000), which contains both the nucleoside and glucose transport proteins. However, they did not recognize the glucose transporter when this was prepared free of nucleoside transporter by expression from a cDNA clone. Their specificity for the nucleoside transporter was confirmed by the ability to immunoadsorb NBMPR- but not cytochalasin B-binding sites from a detergent-solubilized mixture of band 4.5 proteins. Although a large proportion of the antibodies recognized extracellular epitopes, these appeared to be located primarily on the polypeptide moiety of the glycoprotein, as demonstrated by the ability of the antibodies strongly to label the deglycosylated transporter (apparent M(r) 45,000) on Western blots. The antibodies were species-cross-reactive, recognizing nucleoside transporters from pig and rabbit erythrocytes and from rat liver. The pig protein is similar to the human transporter in its inhibitor sensitivity but is considerably larger (apparent M(r) 57,000 after deglycosylation). In contrast, the rat protein is similar in size to the human transporter (apparent M(r) 45,000 after deglycosylation) but much less sensitive to the inhibitors dilazep and dipyridamole. These findings indicate that despite their differences in size and inhibitor specificity, the NBMPR-sensitive nucleoside transporters of these mammalian species are related in amino acid sequence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21954-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1400505-Affinity Labels, pubmed-meshheading:1400505-Animals, pubmed-meshheading:1400505-Antibodies, pubmed-meshheading:1400505-Blood Proteins, pubmed-meshheading:1400505-Blotting, Western, pubmed-meshheading:1400505-Carrier Proteins, pubmed-meshheading:1400505-Cells, Cultured, pubmed-meshheading:1400505-Cross Reactions, pubmed-meshheading:1400505-DNA, pubmed-meshheading:1400505-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:1400505-Erythrocyte Membrane, pubmed-meshheading:1400505-Humans, pubmed-meshheading:1400505-Membrane Proteins, pubmed-meshheading:1400505-Nucleoside Transport Proteins, pubmed-meshheading:1400505-Rabbits, pubmed-meshheading:1400505-Sequence Homology, Nucleic Acid, pubmed-meshheading:1400505-Substrate Specificity, pubmed-meshheading:1400505-Swine, pubmed-meshheading:1400505-Thioinosine
pubmed:year
1992
pubmed:articleTitle
Mammalian nitrobenzylthioinosine-sensitive nucleoside transport proteins. Immunological evidence that transporters differing in size and inhibitor specificity share sequence homology.
pubmed:affiliation
Department of Biochemistry and Chemistry, Royal Free Hospital School of Medicine, University of London, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't