Primary structure of rat thymus prothymosin alpha.
Haritos. A A AA; Blacher. R R; Stein. S S; Caldarella. J J; Horecker. B L BL
Key Findings
- Prothymosin alpha from rat thymus is 113 amino acids long.
- The N‑terminal 28 residues are identical to calf thymosin‑alpha‑1.
- Half of the residues are acidic (dicarboxylic) and cluster in the middle; the protein lacks aromatic and sulfur‑containing amino acids.
- Computer modeling suggests at least five alpha‑helices separated by short random coils.
Practical Outcomes
- For biohackers, this paper provides no direct guidance on using thymosin‑alpha‑1 for longevity, metabolism, or performance. It is purely a structural description, so there are no actionable protocols, dosage recommendations, or safety insights to apply.
Summary
This study just maps out the exact amino‑acid sequence of a rat protein called prothymosin alpha and predicts its shape. It tells us that the first 28 building blocks match the known peptide thymosin‑alpha‑1, but it doesn’t test any health effects or give dosing advice.
Abstract
The primary structure of prothymosin alpha from rat thymus, containing 113 amino acid residues, is reported as follows: (formula; see text) The sequence of the first 28 amino acids at the NH2 terminus is identical to that of calf thymosin alpha 1. The dicarboxylic amino acids, which account for nearly half of the total residues in prothymosin alpha, are largely clustered in the central portion of the polypeptide chain. The polypeptide contains no aromatic or sulfur-containing amino acids. A computer analysis of the three-dimensional structure based on the primary sequence suggests that the molecule is composed of at least five alpha-helical regions interrupted by one short extended chain and three short random coils.
Study Information
pubmed
1985
10.1073/pnas.82.2.343