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Confirmation of the primary structure of thymosin alpha1 by microsequence analysis of limited acid and enzymatic hydrolysis fragments.

作者信息

Michalewsky J, Gabriel T F, Winter D P, Makofske R, Danho W, Shively J, Biemann K, Meienhofer J

出版信息

Int J Pept Protein Res. 1983 Jan;21(1):93-9. doi: 10.1111/j.1399-3011.1983.tb03082.x.

DOI:10.1111/j.1399-3011.1983.tb03082.x
PMID:6826286
Abstract

The primary structure of the 28-peptide thymosin alpha 1 as determined by Goldstein et al. (1) has been 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.

摘要

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