The LKEKK synthetic peptide as a ligand of rat intestinal epithelial cell membranes
| Autor: | Dmitry V. Zinchenko, Yu. A. Zolotarev, Elena V. Navolotskaya, V. I. Vladimirov, A. A. Kolobov, V. B. Sadovnikov |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification 030102 biochemistry & molecular biology Organic Chemistry Adenylate kinase Peptide Biology Ligand (biochemistry) Trypsin Biochemistry Molecular biology Pentapeptide repeat 03 medical and health sciences 030104 developmental biology Membrane chemistry medicine Receptor Cyclase activity medicine.drug |
| Zdroj: | Russian Journal of Bioorganic Chemistry. 42:479-483 |
| ISSN: | 1608-330X 1068-1620 |
| DOI: | 10.1134/s1068162016050137 |
| Popis: | A tritium-labeled synthetic LKEKK pentapeptide corresponding to the sequences 16–20 of human thymosin-α1 and 131–135 of human interferon-α2 was obtained with a specific activity of 28 Ci/mmol. [3H]LKEKK was found to bind with high affinity (K d 3.7 ± 0.3 nM) to the membranes isolated from epithelial cells of rat small intestinal mucosa. The trypsin treatment of the membranes did not affect the binding, thus supporting the nonprotein nature of the peptide receptor. The binding of the labeled peptide was inhibited by unlabeled thymosin-α1, interferon-α2, and cholera toxin B subunit (K i 4.2 ± 0.4, 3.5 ± 0.3, and 4.7 ± 0.3 nM respectively). The pentapeptide did not affect the adenylate cyclase activity within the concentration range of 1–1000 nM. |
| Databáze: | OpenAIRE |
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