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

Autor: Michalewsky J, Gabriel TF, Winter DP, Makofske R, Danho W, Shively J, Biemann K, Meienhofer J
Jazyk: angličtina
Zdroj: International journal of peptide and protein research [Int J Pept Protein Res] 1983 Jan; Vol. 21 (1), pp. 93-9.
DOI: 10.1111/j.1399-3011.1983.tb03082.x
Abstrakt: 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.
Databáze: MEDLINE