Isolation and partial characterization of the major sialoglycoprotein of human T-lymphoblastoid cells of a MOLT-4B cell line.
Isolation and partial characterization of the major sialoglycoprotein of human T-lymphoblastoid cells of a MOLT-4B cell line.
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MOLT-4B 细胞系人 T 淋巴母细胞的主要唾液酸糖蛋白的分离和部分表征。
DOI：
10.1042/bj1750823
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发表时间：
1978
期刊：
影响因子：
--
通讯作者：
T. Osawa
中科院分区：
文献类型：
--
作者：
M. Saito;S. Toyoshima;T. Osawa
一种唾液酸糖蛋白，具有约mol.wt.从人T淋巴细胞来源的MOLT-4 B细胞系的类淋巴母细胞中，通过离子交换层析、麦胚凝集素-琼脂糖柱亲和层析和制备性平板凝胶电泳，分离出95000的人T淋巴细胞。该糖蛋白在细胞表面上的定位通过高碘酸盐/NaB 3 H4和乳过氧化物酶催化的碘化方法的表面标记来指示。该糖蛋白的碳水化合物分析显示，其总碳水化合物含量为28%（w/w），含有岩藻糖、半乳糖、甘露糖、N-乙酰葡萄糖胺、N-乙酰半乳糖胺和唾液酸，摩尔比例为1.0：4.0：3.7：3.5：1.2：2.5，表明它有两种类型的糖链，即与血清糖蛋白相似的糖链和粘蛋白中发现的类型的糖链。实际上，这种糖蛋白的碱性硼氢化物处理产生三糖和四糖，后者除了每个半乳糖分子、N-乙酰半乳糖胺和唾液酸外还含有1个岩藻糖分子。这种糖蛋白结合蓖麻凝集素和伴刀豆球蛋白A以及小麦胚芽凝集素。
A sialoglycoprotein with an approx. mol.wt. of 95000 was isolated from human lymphoblastoid cells of a MOLT-4B cell line, which was of human T-lymphocyte origin, by ion-exchange chromatography, affinity chromatography on a column of wheat-germ agglutinin-Sepharose and preparative slab-gel electrophoresis. The localization of this glycoprotein on the cell surface was indicated by surface labelling by the periodate/NaB3H4 and lactoperoxidase-catalysed iodination methods. Carbohydrate analyses of this glycoprotein revealed that its total carbohydrate content is 28% (w/w), and it contains fucose, galactose, mannose, N-acetylglucosamine, N-acetylgalactosamine and sialic acid in molar proportions 1.0:4.0:3.7:3.5:1.2:2.5, suggesting that it has two types of sugar chain, i.e. sugar chains like those of serum glycoproteins and sugar chains of the type found in mucins. Actually, alkaline borohydride treatment of this glycoprotein yielded tri- and tetra-saccharide, the latter containing 1 molecule of fucose in addition to each molecule of galactose, N-acetylgalactosamine and sialic acid. This glycoprotein bound to Ricinus communis agglutinin and concanavalin A as well as to wheat-germ agglutinin.