Characterization of a hormonogenic domain from human thyroglobulin
- 27 October 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 207 (2) , 302-306
- https://doi.org/10.1016/0014-5793(86)81509-5
Abstract
A polypeptide domain of molecular mass near 22 kDa was purified from CNBr-digest of iodine poor human thyroglobulin (hTgb). This fragment represents the N-terminal part of the hTgb molecule and consequently contains the preferential hormonogenic tyrosine ‘acceptor’ of the protein. This fragment could correspond to the non-iodinated and unreduced form of the thyroxinyl-containing 26 kDa peptide previously purified from reduced and iodinated hTgb. This 22 kDa fragment is capable by itself, i.e. independently of the remaining hTgb molecule, of synthesizing thyroxine with a high efficiency after in vitro iodination. Its study should constitute a valuable way to identify at least one of the hormonogenic tyrosine ‘donor’ residues of hTgbKeywords
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