Studer H, Kneubuehl F, Haeberli A
Endocrinol Exp. 1982 Nov;16(3-4):283-90.
Full reduction of guinea pig thyroglobulin with mercaptoethanol followed by polyacrylamide gel electrophoresis reveals the presence besides the well known three polypeptide chains, of small amounts of iodopeptides with a molecular weight of 3 000 to 46 000 daltons. One of these peptides with a molecular weight of roughly 10 000 daltons has a much higher efficiency to couple iodotyrosines into thyroxine than any other fragment of thyroglobulin. Despite its small quantity this peptide contributes more than one third to the total thyroxine synthesis from a given iodide shot at any time up to five days after its injection. Iodopeptides akin to that found in guinea pigs were recently described by several authors in different species. They probably represent the preferential domains for hormone synthesis within the intact thyroglobulin molecule.
用巯基乙醇将豚鼠甲状腺球蛋白完全还原，随后进行聚丙烯酰胺凝胶电泳，结果显示，除了众所周知的三条多肽链外，还存在少量分子量为3000至46000道尔顿的碘肽。其中一种分子量约为10000道尔顿的肽，将碘酪氨酸偶联成甲状腺素的效率比甲状腺球蛋白的任何其他片段都高得多。尽管其含量很少，但在注射后长达五天的任何时间内，从给定的一次碘注射中合成的总甲状腺素中，这种肽的贡献超过三分之一。最近，几位作者在不同物种中描述了类似于在豚鼠中发现的碘肽。它们可能代表完整甲状腺球蛋白分子内激素合成的优先区域。
