Kishimoto T, Tavassoli M
Anal Biochem. 1986 Mar;153(2):324-9. doi: 10.1016/0003-2697(86)90099-0.
A method is described in which the glycoprotein transferrin was double labeled. Its sialic acid residues were labeled with 3H through a consecutive oxidation-reduction technique utilizing tritiated NaBH4. Its protein moiety was labeled with either 125I or 59Fe. Incubation of this double-labeled molecule at 4 degrees C with K562 cells gave overlapping curves, indicating identical patterns of binding for all labels. At 37 degrees C, 3H and 125I demonstrated identical patterns while 59Fe was cummulatively retained. This method can be used to follow the fate of other glycoproteins and their possible desialation in vivo.
本文描述了一种对糖蛋白转铁蛋白进行双重标记的方法。利用氚化硼氢化钠通过连续氧化还原技术用³H标记其唾液酸残基。其蛋白质部分用¹²⁵I或⁵⁹Fe进行标记。将这种双重标记的分子在4℃下与K562细胞一起温育，得到重叠曲线，表明所有标记物的结合模式相同。在37℃时，³H和¹²⁵I表现出相同的模式，而⁵⁹Fe则被累积保留。该方法可用于追踪其他糖蛋白在体内的命运及其可能的去唾液酸化过程。
