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An extract of a tumour metastases from a human medullary thyroid carcinoma contained a high concentration (at least 2·9 nmol/g wet weight) of the immunoregulatory peptide, thymosin-β4. The peptide was isolated as a mixture of two components with free and blocked NH₂-terminal amino acid residues, the latter form predominating (approximately 98% of the total). The primary structure of the peptide was established by automated Edman degradation after cleavage with cyanogen bromide. The amino acid sequence of human thymosin-β₄ was identical to thymosin-β₄ previously isolated from calf thymus. Further studies are warranted to determine whether thymosin-β₄ production is a useful marker for thyroid and other tumours.

J. Endocr. (1988) 118, 155–159

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