Blok J, Mulder-Stapel A A, Ginsel L A, Daems W T
Histochemistry. 1980;69(2):131-5. doi: 10.1007/BF00533129.
The binding of cationized ferritin (CF) to the cell-coat (glycocalyx) glycoproteins of human and rat intestinal absorptive cells was investigated in relation to the amount of sialic acid in these macromolecules. The cell coat of human absorptive cells exhibited poor binding of CF and contained a small amount of sialic acid. The cell coat of rat absorptive cells had about ten times more sialic acid than that of human cells and showed a strong affinity for the marker. The removal of sialic acid from the cell-coat glycoproteins of rat intestinal cells by neuraminidase treatment abolished CF binding. These results suggest that sialic acid is necessary for CF binding and that human and rat intestinal absorptive cells show a species-specific difference in the sugar composition of the cell coat.
研究了阳离子铁蛋白（CF）与人及大鼠肠道吸收细胞的细胞被（糖萼）糖蛋白的结合情况，并与这些大分子中唾液酸的含量相关。人吸收细胞的细胞被对CF的结合能力较差，且含有少量唾液酸。大鼠吸收细胞的细胞被中唾液酸的含量是人细胞的约十倍，且对该标记物表现出很强的亲和力。用神经氨酸酶处理大鼠肠道细胞的细胞被糖蛋白以去除唾液酸后，CF的结合消失。这些结果表明唾液酸是CF结合所必需的，且人和大鼠肠道吸收细胞在细胞被的糖组成上表现出种属特异性差异。
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