Primary structure of thymosin beta 12, a new member of the beta-thymosin family isolated from perch liver.
Low. T L TL; Liu. D T DT; Jou. J H JH
Key Findings
- Thymosin beta 12 is a 43‑residue peptide weighing 4822 Da
- Its N‑terminus is acetyl‑blocked
- It shares 79% similarity with thymosin beta 4 and 84% with thymosin beta 11
Practical Outcomes
- The discovery doesn’t give any dosage or benefit information, so there’s no immediate use for self‑experimenters. It mainly adds to basic knowledge of fish peptides.
Summary
Scientists found a new 43‑amino‑acid peptide called thymosin beta 12 in perch liver. It’s similar to the well‑known thymosin beta 4 but they only described its structure, not any health effects.
Abstract
A new polypeptide termed thymosin beta 12 has been isolated from perch liver and its primary structure elucidated. This polypeptide contains 43 amino acid residues with a molecular weight of 4822 Da. The content of thymosin beta 12 from perch liver has been determined as 43 micrograms/g of tissue. The amino-terminal end of this polypeptide is blocked by an acetyl group as deciphered by fast-atom bombardment mass spectrometric analysis. Sequence analysis reveals that thymosin beta 12 is 79% homologous to thymosin beta 4, an immunomodulator which was originally isolated from calf thymus. Thymosin beta 12 also shows 84% sequence homology to thymosin beta 11, a beta 4 analog which replaces beta 4 in two species of bony fish, oscar and rainbow trout. The evolutionary implication of such results will be discussed. The isolation of a new beta 4-related peptide from perch liver which differs from beta 11 indicates that beta-thymosin peptides are widely distributed in lower vertebrate classes.
Study Information
pubmed
1992
1992-02-14T00:00:00.000Z
10.1016/0003-9861(92)90361-y