Rhodes S B, Frantz W L, Holland J
Biochem Biophys Res Commun. 1984 Jun 15;121(2):686-94. doi: 10.1016/0006-291x(84)90236-5.
A completely iodinated form of ovine prolactin was prepared using lactoperoxidase. The iodination was characterized using gel filtration, electrophoresis and fluorescence analysis. Complete iodination corresponds to a 33% decrease in intrinsic tryptophanyl fluorescence (275 parallel 348). Each ovine prolactin molecule possesses four iodination sites which cannot be distinguished by kinetic analysis. The receptor binding capacity of the tetraiodoprolactin was also assayed using the particulate fraction from female rat livers. Although the total binding capacity of native and iodoprolactins is indistinguishable, significant differences in receptor binding behavior were observed.
使用乳过氧化物酶制备了完全碘化形式的绵羊催乳素。通过凝胶过滤、电泳和荧光分析对碘化过程进行了表征。完全碘化对应于内在色氨酸荧光（275与348平行）降低33%。每个绵羊催乳素分子具有四个碘化位点，动力学分析无法区分这些位点。还使用来自雌性大鼠肝脏的微粒部分测定了四碘催乳素的受体结合能力。尽管天然催乳素和碘化催乳素的总结合能力无法区分，但在受体结合行为上观察到了显著差异。
