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  • Title: Characterization of a hormonogenic domain from human thyroglobulin.
    Author: Marriq C, Lejeune PJ, Venot N, Rolland M, Lissitzky S.
    Journal: FEBS Lett; 1986 Oct 27; 207(2):302-6. PubMed ID: 3770203.
    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 hTgb.
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