FEBS Letters | |
On the molecular size of thymosins | |
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
【 预 览 】
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RO201912020289381ZK.pdf | 378KB | download |