Synthetic peptide SLTCLVKGFY competes with β-endorphin for naloxone-insensitive binding sites on rat brain membranes
| Autor: | Valery M. Lipkin, Natalia Malkova, T. A. Zargarova, Elena V. Navolotskaya, Vladimir P. Zav'yalov, S. B. Krasnova |
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| Rok vydání: | 2002 |
| Předmět: |
Enkephalin
Physiology Immunoglobulin gamma-Chains Narcotic Antagonists Molecular Sequence Data Peptide (+)-Naloxone Ligands Binding Competitive Biochemistry Cellular and Molecular Neuroscience Endocrinology Animals Amino Acid Sequence Binding site Receptor Binding selectivity chemistry.chemical_classification Binding Sites Dose-Response Relationship Drug Naloxone Chemistry Cell Membrane beta-Endorphin Brain Peptide Fragments Protein Structure Tertiary Rats Cortex (botany) Kinetics Membrane Immunoglobulin G Biophysics Immunoglobulin Constant Regions Peptides Oligopeptides Protein Binding |
| Zdroj: | Peptides. 23:1115-1119 |
| ISSN: | 0196-9781 |
| Popis: | The synthetic decapeptide Ser–Leu–Thr–Cys–Leu–Val–Lys–Gly–Phe–Tyr (termed immunorphin) corresponding to the sequence 364–373 of the CH3 domain of human immunoglobulin G heavy chain and its synthetic fragment VKGFY were found to compete with 125 I -labeled β-endorphin for high-affinity naloxone-insensitive binding sites on membranes isolated from the rat brain cortex (Ki=1.18±0.09 and 1.58±0.11 nM, respectively). The binding specificity study revealed that these binding sites were insensitive not only to naloxone but to [Met5]enkephalin and [Leu5]enkephalin as well. The Kd values characterizing the specific binding of 125 I -labeled immunorphin and its fragment Val–Lys–Gly–Phe–Tyr to these binding sites were determined to be 2.93±0.27 nM and 3.17±0.29 nM, respectively. |
| Databáze: | OpenAIRE |
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