Matsunaga E, Shinkai H
Arch Dermatol Res. 1985;277(2):93-7. doi: 10.1007/BF00414104.
A new acidic glycoprotein was isolated from 4 M-guanidiunium chloride which had been extracted from neutral-salt-insoluble fractions of neonatal calf skin. During the process of purification, the glycoprotein co-migrated with proteodermatan sulphate and its sugar components mainly consisted of fucose, mannose and hexosamine. A broad band obtained by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis suggested that the molecular weight was 100,000. High-voltage electrophoresis, revealed acidic fragments in its tryptic peptides, while its oligosaccharide chains were shown to have on acidic nature by electrophoresis on a cellulose acetate membrane. These results show that the glycoprotein differs from other glycoproteins (fibronectin, laminin, entactin, nidogen and the 31-K protein of chondrocyte membrane) which have been reported in connective tissues.
从新生小牛皮肤中性盐不溶性组分中提取的4M - 胍盐酸盐中分离出一种新的酸性糖蛋白。在纯化过程中，该糖蛋白与蛋白聚糖硫酸酯共同迁移，其糖成分主要由岩藻糖、甘露糖和己糖胺组成。十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶电泳得到的宽条带表明分子量为100,000。高压电泳显示其胰蛋白酶肽段中有酸性片段，而其寡糖链在醋酸纤维素膜上电泳显示具有酸性性质。这些结果表明该糖蛋白不同于结缔组织中已报道的其他糖蛋白（纤连蛋白、层粘连蛋白、巢蛋白、巢蛋白原和软骨细胞膜的31-K蛋白）。
