Isolation and structural characterization of thymosin-β4 from a human medullary thyroid carcinoma

Abstract

ABSTRACT 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