Abstract
IN an investigation of the N-terminal amino-acids in hog thyroglobulin, purified by ammonium sulphate fractionation1, Roche et al.2,3 found that the wide range of amino-acids which they detected by application of the Edman4 and Sanger5 methods included di-iodotyrosine and thyroxine. These observations could emphasize a role for thyroid leucine aminopeptidase6,7 in the mechanism governing the release of the thyroid hormone from its stored form in the thyroid gland. We have also been concerned with this physiological process8 and have re investigated the N-terminal groups in the purified thyroid protein.
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References
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DOPHEIDE, T., TRIKOJUS, V. N-Terminal Amino-acids in Purified Hog Thyroglobulin. Nature 201, 1128–1129 (1964). https://doi.org/10.1038/2011128a0
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DOI: https://doi.org/10.1038/2011128a0
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