On the molecular size of thymosins

FEBS Letters

Felix, A.M.³  Heimer, E.P.³  Yialouris, P.P.²  Haritos, A.A.²  Rosemeyer, M.A.¹ 

[1] Department of Biochemistry, University College London, Gower Street, London WC1E 6BT, England;Zoological Laboratory, Faculty of Science, University of Athens, GR 157 84 Athens, Greece;Peptide Research Department, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ 07110, USA

关键词: Thymosin α1;    Prothymosin α;    Sedimentation equilibrium;    Gel filtration;   

DOI  :  10.1016/0014-5793(87)81028-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The immunoregulatory polypeptide prothymosin α and its biologically active N-terminal fragment thymosin α₁m, 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 α, thymosin β₄ and thymosin β₁₀. In contrast, sedimentation equilibrium ultracentrifugation shows that thymosin α₁ is a monomer with a relative molecular mass of 3000±200. Measurement of the diffusion coefficient as 221 μm²/s suggests that the molecule is approximately spherical. The implications for the molecular species of prothymosin α, parathymosin α, and β-thymosins are discussed.

【 授权许可】

Unknown