Interaction of Synthetic Dipeptide Bestim with Mouse Thymocytes and Macrophages

Autor:	Cynthia Tuthill, Nikolai I. Kolodkin, Yury A. Zolotarev, Elena V. Navolotskaya, Kolobov Alexander A
Rok vydání:	2007
Předmět:	Dipeptide Adenylate kinase Bioengineering Trypsin Biochemistry Molecular biology Analytical Chemistry chemistry.chemical_compound Thymocyte Membrane chemistry Drug Discovery medicine Molecular Medicine Specific activity Receptor Cyclase activity medicine.drug
Zdroj:	International Journal of Peptide Research and Therapeutics. 14:97-103
ISSN:	1573-3904 1573-3149
DOI:	10.1007/s10989-007-9111-2
Popis:	Tritium-labeled dipeptide bestim (γ-D-Glu-L-Trp) with a specific activity of 45 Ci/mmol was obtained by the high-temperature solid-state catalytic isotope exchange (HSCIE) reaction. [3H]bestim was found to bind with high affinity to mouse peritoneal macrophages (K d 2.1 ± 0.1 nM) and thymocytes (K d 3.1 ± 0.2 nM) and also plasma membranes isolated from these cells (K d 18.6 ± 0.2 and 16.7 ± 0.3 nM respectively). The specific bonding of [3H]bestim with macrophages and thymocytes was inhibited by unlabeled dipeptide thymogen (L-Glu-L-Trp) (K i 0.9 ± 0.1 and 1.1 ± 0.1 nM respectively). Treatment of the macrophages and thymocytes with trypsin led to their loss of capacity to bind [3H]bestim. Bestim at concentrations range of 0.1–1000 nМ reduced the adenylate cyclase activity in macrophage and thymocyte membranes.
Databáze:	OpenAIRE
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