Muramatsu H, Muramatsu T, Avner P
Cancer Res. 1982 May;42(5):1749-52.
The present study deals with the biochemical properties of high-molecular-weight glycopeptides isolated from the surface of human teratocarcinoma cells. This cell surface material released by mild trypsin digestion from galactose-labeled human teratocarcinoma cells, Tera I and PA1, was digested extensively with pronase. Most of the resulting glycopeptides were large and were excluded from a Sephadex G-50 column. The properties of these large cell surface glycopeptides isolated from Tera I cells have been examined in detail. It is clear from these experiments that they are neither acidic mucopolysaccharides nor mucin-type glycopeptides with short oligosaccharide chains. Although the glycopeptides are hardly hydrolyzed by beta-galactosidase even after prior digestion with neuraminidase, around 30% of the glycopeptides are depolymerized by treatment with endo-beta-galactosidase from Escherichia freundii. The large cell surface glycopeptides from Tera I cells therefore appear to be very similar to the large glycopeptides seen on mouse embryonal carcinoma cells, which have core structures composed of galactose and N-acetylglucosamine. Like the mouse cell glycopeptides, a fraction of the large glycopeptides from these human cells bind to agarose-conjugated fucose-binding proteins and peanut agglutinin.
本研究涉及从人畸胎瘤细胞表面分离出的高分子量糖肽的生化特性。通过温和的胰蛋白酶消化从半乳糖标记的人畸胎瘤细胞Tera I和PA1释放的这种细胞表面物质，用链霉蛋白酶进行了广泛消化。大多数所得糖肽分子量较大，不能通过Sephadex G - 50柱。已详细研究了从Tera I细胞分离出的这些大细胞表面糖肽的特性。从这些实验中可以清楚地看出，它们既不是酸性粘多糖，也不是具有短寡糖链的粘蛋白型糖肽。尽管即使在用神经氨酸酶预先消化后，糖肽也几乎不被β - 半乳糖苷酶水解，但约30%的糖肽在用弗氏埃希菌的内切β - 半乳糖苷酶处理后会发生解聚。因此，来自Tera I细胞的大细胞表面糖肽似乎与在小鼠胚胎癌细胞上看到的大糖肽非常相似，后者具有由半乳糖和N - 乙酰葡糖胺组成的核心结构。与小鼠细胞糖肽一样，这些人细胞中的一部分大糖肽与琼脂糖偶联的岩藻糖结合蛋白和花生凝集素结合。
