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According to gel-filtration experiments, α- and β-thymosins appear to form oligomers, which are 4-5-fold larger than the corresponding polypeptides. However, on analysis by sedimentation equilibrium ultracentrifugation, prothymosin α and thymosin β 4 showed relative molecular masses of 12 800 and 4600, which are close to the values calculated from their amino acid sequences, confirming their...
The immunoregulatory polypeptide prothymosin α and its biologically active N-terminal fragment thymosin α 1 m, 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 β ...
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