Characterization of a hormonogenic domain from human thyroglobulin

FEBS Letters
C MarriqS Lissitzky

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.

References

Dec 17, 1985·Biochemical and Biophysical Research Communications·S FormisanoR Di Lauro
Apr 15, 1983·Biochemical and Biophysical Research Communications·C MarriqS Lissitzky
Oct 15, 1980·The Biochemical Journal·M J OwenM J Crumpton
Oct 1, 1980·European Journal of Biochemistry·C MarriqS Lissitzky

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Citations

Jan 30, 1990·Biochemical and Biophysical Research Communications·J L FrancC Marriq
Feb 1, 1989·Biochimie·Y MalthièryS Lissitzky

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