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新生大鼠表皮细胞中岩藻糖基转移酶活性的分化变化。

Differentiative changes in fucosyltransferase activity in newborn rat epidermal cells.

作者信息

Xiang J, Bernstein I A

机构信息

Department of Environmental and Industrial Health, The University of Michigan, Ann Arbor 48109-2029.

出版信息

Biochem Biophys Res Commun. 1992 Nov 30;189(1):27-32. doi: 10.1016/0006-291x(92)91520-z.

Abstract

An enzymatic activity catalyzing the transfer of L-fucose from GDP-L-fucose to a glycoprotein that is associated with the surfaces of the basal cells has been found in the membranous fraction of the cutaneous epidermis from the newborn rat. This fucosyltransferase which is located in the differentiated cells alters the acceptor glycoprotein's lectin-binding specificity from the Isolectin I-B4 of Griffonia simplicifolia (GS I-B4) to the Agglutinin I of Ulex europeus (UEA) and could be responsible for the same change in lectin-binding specificity that occurs as the epidermal basal cell differentiates. Another membraneous fucosyltransferase that can use asialofetuin--but not the GS I-B4-binding glycoprotein--as an acceptor, is also present in the membraneous fraction.

摘要

在新生大鼠皮肤表皮的膜部分中发现了一种酶活性,该酶活性催化L-岩藻糖从GDP-L-岩藻糖转移至与基底细胞表面相关的糖蛋白上。这种位于分化细胞中的岩藻糖基转移酶可将受体糖蛋白的凝集素结合特异性从简单叶豆凝集素I-B4(GS I-B4)转变为欧洲荆豆凝集素I(UEA),并且可能是表皮基底细胞分化时发生的凝集素结合特异性相同变化的原因。膜部分中还存在另一种膜岩藻糖基转移酶,它可以使用去唾液酸胎球蛋白(而非与GS I-B4结合的糖蛋白)作为受体。

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