PMID: 3384098Jun 20, 1988Paper

Isolation and partial characterization of prothymosin alpha from porcine tissues

FEBS Letters
M EconomouO Tsolas

Abstract

Prothymosin alpha, an immunoactive polypeptide of 12 kDa, has been isolated from porcine thymus, spleen, lung and kidney. It lacks aromatic and sulfur-containing amino acids and has a high content of glutamic and aspartic acids. Tryptic digestion of porcine thymus prothymosin alpha yielded peptides which on separation, amino acid analysis and alignment with the known sequence of prothymosin alpha from rat and man showed that the amino terminal portion of the molecule is conserved and the few differences present are confined to the carboxy terminal.

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Citations

Jun 15, 1996·European Journal of Biochemistry·K VareliM Frangou-Lazaridis
Jan 1, 1993·Virchows Archiv. A, Pathological Anatomy and Histopathology·M FragaJ Forteza
May 23, 1994·FEBS Letters·T Papamarcaki, O Tsolas
Oct 23, 1997·The Journal of Biological Chemistry·R H WangS L Berger
Nov 15, 1996·European Journal of Biochemistry·K KondiliT Papamarcaki
Jan 7, 2000·Journal of Cellular Physiology·S A EnkemannS L Berger
Jan 1, 1997·Life Sciences·C L WuC S Lin
Jul 1, 1992·Archives of Biochemistry and Biophysics·S FrillingosO Tsolas
May 4, 1993·Biochemistry·A R SburlatiS L Berger

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