Preparation of biologically active radioiodinated thymopentin
β Scribed by Krish Venkat; John Tischio; Jonathan Crowther; Tapan Audhya; Gideon Goldstein
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- French
- Weight
- 232 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0022-2135
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β¦ Synopsis
Abstract
Thymopentin (TP5, ArgβLysβAspβValβTyr), a synthetic pentapeptide corresponding to amino acids 32β36 of the thymic hormone thymopoietin, has the biological activity of the parent compound. The tyrosyl residue was iodinated using the chloramineβT method and the reaction mixture separated by HPLC into peaks corresponding to free TP5, monoβiodo TP5 and diβiodo TP5, identified by mass spectrometry. Biological activity was retained in the iodinated peptides but, surprisingly, free TP5 had lost biological activity during the separation process. The biologically active monoiodinated TP5 had a specific activity of 28 ΞΌCi/ΞΌg and will be useful in studies of receptor binding.
π SIMILAR VOLUMES
The solution conformation of the pentapeptide Arg-Pro-Asp-Val-Tyr ( [Pro2]TP5), a biologically active analog of the immunoregulatory peptide thymopentin, Arg-Lys-Asp-Val-Tyr (TP5). was investigated by proton nuclear magnetic resonance spectroscopy. The chemical shift variations with pH, the vicinal