Structure and immunological properties of thymosin β9 Met, a new analog of thymosin β4 isolated from porcine thymus

TERESA L.K. LOW*, CHING‐YUANG ‐Y LIN, TAIR‐LONG ‐L PAN, AIH‐JING ‐J CHIOU, AKIRA TSUGITA

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

9 Scopus citations

Abstract

During the course for the studies of thymosin β4 and prothymosin α from porcine thymus, a new analog of thymosin β4 has been identified. This peptide consists of 41 amino acid residues. The amino terminus is blocked by an acetyl group as revealed by fast atom bombardment mass spectrometric analysis. Amino acid sequence studies disclosed that this peptide is identical to bovine thymosin β9 except that leucine at position 6 in β9 is substituted by methionine. Thus, this new peptide has been termed thymosin β9 Met. The recoveries of β9Met, β4, and prothymosin α in porcine tissues have been determined (in μg/g tissue) as follows: thymus (43, 85, 133); spleen (68, 203, 37); liver (10, 31, 27); heart (1.5, 10, 0); kidney (5, 51, 37); brain (0.8, 31, 5). Biologically, thymosin β9 Met was found to be more active than β4 in enhancing γ‐interferon production in cord blood lymphocytes. However, β4 appeared to stimulate higher amounts of interleukin 2 and tumor necrotic factor. The significance for the coexistence of two homologous peptides with similar functions in the thymus and a number of other organs is not clear, and deserves further investigation.

Original languageEnglish
Pages (from-to)481-488
Number of pages8
JournalInternational Journal of Peptide and Protein Research
Volume36
Issue number6
DOIs
StatePublished - 12 1990
Externally publishedYes

Keywords

  • immunomodulators
  • porcine thymus
  • structure
  • thymic hormones
  • thymosin β
  • thymosin β Met

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