On the molecular size of thymosins.
Haritos. A A AA; Yialouris. P P PP; Heimer. E P EP; Felix. A M AM; Rosemeyer. M A MA
Key Findings
- Thymosin alpha‑1 has a molecular mass of roughly 3,000 daltons.
- Gel‑filtration suggested it might form groups, but ultracentrifugation proved it stays as a monomer.
- Its shape is roughly spherical, based on diffusion measurements.
Practical Outcomes
- Knowing that thymosin alpha‑1 is a monomer helps users calculate accurate doses and anticipate that it won't spontaneously aggregate, which can affect stability and formulation. This information is mainly confirmatory and doesn’t change how the peptide is taken, but it reassures that standard dosing based on its 3 kDa size is appropriate.
Summary
The study shows that the peptide thymosin alpha‑1 is a single, small protein (about 3 kDa) that behaves as a single unit in solution, not as a cluster of molecules.
Abstract
The immunoregulatory polypeptide prothymosin alpha and its biologically active N-terminal fragment thymosin alpha 1m, with relative molecular masses of 12,500 and 3108 respectively, were found to behave as oligomers (trimers to hexamers) in gel-filtration measurements. This phenomenon of an apparent association of polypeptides has been reported for other thymosins--parathymosin alpha, thymosin beta 4 and thymosin beta 10. In contrast, sedimentation equilibrium ultracentrifugation shows that thymosin alpha 1 is a monomer with a relative molecular mass of 3000 +/- 200. Measurement of the diffusion coefficient as 221 micron2/s suggests that the molecule is approximately spherical. The implications for the molecular species of prothymosin alpha, parathymosin alpha, and beta-thymosins are discussed.
Study Information
pubmed
1987
1987-06-22T00:00:00.000Z
10.1016/0014-5793(87)81028-1
15
32