Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1995-6-21
|
| pubmed:abstractText |
125I-labelled recombinant human interferon alpha 2 (rHuIFN-alpha 2) capable of high-affinity binding (Kd = 2.46 +/- 0.18 x 10(-10) M) with receptors expressed on mouse thymocytes was obtained. Prothymosin alpha (proTM-alpha) but not cholera toxin was found to compete with radiolabelled IFN-alpha 2 for binding to the same receptor (Ki = 3.68 +/- 0.21 x 10(-11) M). The synthetic peptide covering the sequence 130-137 of IFN-alpha 2 (authors' definition: alpha-peptoferon) was shown to have the capacity to displace the labelled IFN-alpha 2 from the IFN-alpha 2/receptor complex (Ki = 7.19 +/- 0.12 x 10(-11) M). It was shown that receptors of this type are localized in plasmatic membrane fraction. Using [125I]-alpha-peptoferon, specific and saturable binding was detected on human fibroblasts and the data fitted a single binding site. Scatchard analysis yielded a Kd of 9.63 +/- 0.17 x 10(-8) M. The binding was competitively inhibited by IFN-alpha 2 (the Ki value in competition assays was 1.37 +/- 0.12 x 10(-8) M), proTM-alpha(Ki = 2.2 +/- 0.2 x 10(-7) M) and cholera toxin B subunit (Ki = 5.5 +/- 0.2 x 10(-7)). The present study has demonstrated that the sequence 130-137 of HuIFN-alpha 2 is involved in the competition of HuIFN-alpha 2, proTM-alpha and cholera toxin B subunit for common receptors on human fibroblasts.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Thymosin,
http://linkedlifedata.com/resource/pubmed/chemical/prothymosin alpha
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0161-5890
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
32
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
425-31
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7753051-Amino Acid Sequence,
pubmed-meshheading:7753051-Animals,
pubmed-meshheading:7753051-Binding, Competitive,
pubmed-meshheading:7753051-Cholera Toxin,
pubmed-meshheading:7753051-Fibroblasts,
pubmed-meshheading:7753051-Humans,
pubmed-meshheading:7753051-Interferon-alpha,
pubmed-meshheading:7753051-Kinetics,
pubmed-meshheading:7753051-Mice,
pubmed-meshheading:7753051-Mice, Inbred CBA,
pubmed-meshheading:7753051-Molecular Sequence Data,
pubmed-meshheading:7753051-Peptides,
pubmed-meshheading:7753051-Protein Precursors,
pubmed-meshheading:7753051-Protein Structure, Tertiary,
pubmed-meshheading:7753051-Receptors, Cell Surface,
pubmed-meshheading:7753051-Sequence Alignment,
pubmed-meshheading:7753051-Sequence Homology, Amino Acid,
pubmed-meshheading:7753051-Thymosin,
pubmed-meshheading:7753051-Thymus Gland
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
The sequence 130-137 of human interferon-alpha 2 is involved in the competition of interferon, prothymosin alpha and cholera toxin B subunit for common receptors on human fibroblasts.
|
| pubmed:affiliation |
Institute of Immunology, Lyubuchany, Chekhov District, Moscow Region, Russia.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|