Ku W W, Bernstein I A
Biochem Biophys Res Commun. 1985 Oct 15;132(1):269-76. doi: 10.1016/0006-291x(85)91018-6.
The cell surface of the newborn rat epidermis exhibits a discrete change in lectin-binding specificity from Griffonia simplicifolia I-B4 (GS I-B4), specific for alpha-D-galactosyl residues, to Ulex europeus agglutinin I (UEA), specific for alpha-L-fucose, as the cell leaves the basal layer and differentiates. It has been postulated that this change is a result of the addition of alpha-L-fucose to nonreducing terminal alpha-D-galactosyl residues on GS I-B4-binding cell surface glycoproteins. If this were the sole nature of the conversion, the physical properties of isolated GS I-B4- and UEA-bound glycoproteins should not differ greatly. UEA and GS I-B4-binding glycoproteins isolated from newborn rat epidermis have similar charge properties and are similar in the nature of their carbohydrate moieties, supporting the proposed hypothesis.
新生大鼠表皮细胞表面的凝集素结合特异性呈现出离散变化,即当细胞离开基底层并开始分化时,从对α-D-半乳糖基残基具有特异性的单叶豆凝集素I-B4(GS I-B4)转变为对α-L-岩藻糖具有特异性的欧洲荆豆凝集素I(UEA)。据推测,这种变化是由于在GS I-B4结合的细胞表面糖蛋白的非还原末端α-D-半乳糖基残基上添加了α-L-岩藻糖所致。如果这是转化的唯一本质,那么分离出的与GS I-B4和UEA结合的糖蛋白的物理性质应该不会有太大差异。从新生大鼠表皮中分离出的与UEA和GS I-B4结合的糖蛋白具有相似的电荷性质,并且其碳水化合物部分的性质也相似,这支持了上述假设。