Isolation and structural characterization of thymosin-beta 4 from a human medullary thyroid carcinoma.
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-beta 4. 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-beta 4 was identical to thymosin-beta 4 previously isolated from calf thymus. Further studies are warranted to determine whether thymosin-beta 4 production is a useful marker for thyroid and other tumours.
Conlon
J M
JM
Clinical Research Group for Gastrointestinal Endocrinology, Max-Planck-Gesellschaft, University of Göttingen, F.R.G.
Grimelius
L
L
Wallin
G
G
Thim
L
L
D000328:Adult; D002277:Carcinoma / Q000032:analysis* / Q000473:pathology; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008297:Male; D013947:Thymosin / Q000031:analogs & derivatives* / Q000302:isolation & purification / Q000378:metabolism; D013964:Thyroid Neoplasms / Q000032:analysis* / Q000473:pathology; D000099201:Thymosin beta(4)
D013947:Thymosin; D000099201:Thymosin beta(4)