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The synthesis is described of an N-terminal thyroglobulin (Tg) polypeptide of 27 kDa, which is capable of hormonogenesis, in a baculovirus system. This polypeptide was made using a 657 bp Tg cDNA cloned from human thyroid RNA by a polymerase chain reaction method. The cDNA contained the information for the Tg signal peptide, the N-terminally located site for thyroid hormone formation and, at the 3' end, a sequence coding for six histidine residues. The fragments produced were purified using a nickel—nitrilotriacetic acid column using these six histidine residues. The products were analysed by sodium dodecyl sulphatepolyacrylamide gel electrophoresis and showed two glycosylated fragments of 32 and 34 kDa, both of which started with asparagine. Iodination of the fragments with lactoperoxidase in vitro resulted in the formation of thyroxine (T₄). The formation rate of T₄ in the fragments was about five times lower than that of the mature Tg dimer of 660 kDa, but ten times more rapid than in bovine serum albumin under the same conditions.

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				P. A. Piosik, M. van Groenigen, J. van Doorn, F. Baas, and J. J. M. de Vijlder Effects of Maternal Thyroid Status on Thyroid Hormones and Growth in Congenitally Hypothyroid Goat Fetuses during the Second Half of Gestation Endocrinology, January 1, 1997; 138(1): 5 - 11. [Abstract] [Full Text] [PDF]