THYROID HORMONE INTERACTIONS WITH CELLS AND PROTEINS

甲状腺素（T4）与载脂蛋白结合的持续研究 专注于纯化的apoE 斯卡查德分析显示，一个单一的网站， Kd约为33 nM，对T4的亲和力大于对T3的亲和力。 通过光亲和性 标记，T4位点定位于N-末端，外显子3编码区 (aa 1-62）。 研究还表明，各种载脂蛋白的活性不同， 对脂质和抑制T4结合的药物的敏感性， 当载脂蛋白掺入脂蛋白时， 粒子 在改进亲和标记物的制备方法中， 甲状腺素和N-溴乙酰基-3，5，3 '-三碘甲状腺原氨酸， 开发了通过逆流色谱法的纯化。 闪光辐射已被用于将全反式视黄酸转化为 异构体的混合物，然后可以通过HPLC进行纯化。 当前注意力 集中于纯化9-顺式视黄酸， 在商业上。

Continuing investigation of thyroxine (T4) binding to apolipoproteins focused on purified apoE. Scatchard analysis revealed a single site with Kd ~33 nM and a greater affinity for T4 than for T3. By photoaffinity labeling, the T4 site was localized to the N-terminal, exon 3-coded region (aa 1-62). It was also shown that various apolipoproteins differ in their sensitivity to lipids and drugs that inhibit T4 binding, and that T4 binding is affected when the apoprotein is incorporated in the lipoprotein particles. In improving the methods for preparing the affinity labels, N-bromoacetyl thyroxine and N-bromoacetyl-3,5,3'-triiodothyronine, a novel principle of purification by countercurrent chromatography was developed. Flash irradiation has been used to convert all-trans retinoic acid to a mixture of isomers, which can then be purified by HPLC. Current attention is focused on purification of 9-cis retinoic acid which is not available commercially.