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- Publisher
- Wiley
- Copyright
- Copyright © 1997 Wiley Subscription Services
- ISSN
- 1075-2617
- eISSN
- 1099-1387
- DOI
- 10.1002/(SICI)1099-1387(199707)3:4<282::AID-PSC119>3.0.CO;2-A
- Publisher site
- See Article on Publisher Site
Abstract
The study of the phylogenetic distribution of the β‐thymosin family is important to elucidate its biological function further. A new thymosin, designated as thymosin β14, consisting of 40 amino acid residues and with a molecular weight of 4537 Da as determined by ion spray mass spectrometry, was isolated from the sea urchin. The N‐terminus of this polypeptide is blocked by an acetyl group as found by matrix‐assisted laser desorption mass spectrometric and amino acid analysis. The primary structure was elucidatd by Edman degradation of the HPLC‐purified thymosin β14 fragments produced by digestion with endoproteinase Asp‐N and trypsin. Sequence comparison reveals that thymosin β14 is 73% homologous to thymosin β4, obtained from calf thymus. By isolating and characterising the structure of thymosin β14 from the sea urchin, an invertebrate, substantial knowledge about the phylogenetic distribution and evolution of β‐thymosins is gained. © 1997 European Peptide Society and John Wiley & Sons Ltd.
Journal
Journal of Peptide Science – Wiley
Published: Jan 1, 1997
Keywords: ; ; ; ;