Confirmation of the primary structure of thymosin α1 by microsequence analysis of limited acid and enzymatic hydrolysis fragments
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 21 (1) , 93-99
- https://doi.org/10.1111/j.1399-3011.1983.tb03082.x
Abstract
The primary structure of the 28-peptide thymosin .alpha.1 as determined by Goldstein et al. was confirmed by independent procedures. Limited dilute acid digestion generated a 26-peptide and a 22-peptide both extending to the C-terminal and lacking the N-terminal blocking group. A combination of Edman microsequencing, carboxypeptidase Y and thermolysin digestion, and fast atom bombardment mass spectrometry was used.Keywords
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