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The 5′‐end of bovine thyroglobulin mRNA encodes a hormonogenic peptide
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The sequence of 370 bases at the 5′‐end of bovine thyroglobulin mRNA has been determine. A41 base untranslated segment was found preceeding the ATG initiator codon. It is followed by an open reading frame providing the first data on thyroglobulin primary structure. Analysis of the amino acid sequence demonstrated the presence of an 18 residue hydrophobic segment representing a putative signal peptide. Comparison of the amino terminal sequence of thyroglobulin with that of peptides known to contain thyroid hormones [7,8] demonstrated that the first tyrosine in native thyroglobulin is mainly found as thyroxine in the mature iodinated protein [8]. Our results clearly identify the amino‐terminal region of thyroglobulin as an important hormonogenic domain of the protein.
Title: The 5′‐end of bovine thyroglobulin mRNA encodes a hormonogenic peptide
Description:
The sequence of 370 bases at the 5′‐end of bovine thyroglobulin mRNA has been determine.
A41 base untranslated segment was found preceeding the ATG initiator codon.
It is followed by an open reading frame providing the first data on thyroglobulin primary structure.
Analysis of the amino acid sequence demonstrated the presence of an 18 residue hydrophobic segment representing a putative signal peptide.
Comparison of the amino terminal sequence of thyroglobulin with that of peptides known to contain thyroid hormones [7,8] demonstrated that the first tyrosine in native thyroglobulin is mainly found as thyroxine in the mature iodinated protein [8].
Our results clearly identify the amino‐terminal region of thyroglobulin as an important hormonogenic domain of the protein.
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