Isolation and partial characterization of prothymosin α from porcine tissues

Authors:
  • OTO. Tsolas
    O. Tsolas

Abstract
Prothymosin α, 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 α yielded peptides which on separation, amino acid analysis and alignment with the known sequence of prothymosin α from rat and man showed that the amino terminal portion of the molecule is conserved and the few differences present are confined to the car☐y terminal.

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