Sheldrake R F, Crocker B D, Husband A J, Rostas J A
Res Vet Sci. 1987 May;42(3):358-64.
Standard methods for the purification of Thy-1 were applied to sheep brain to purify a sheep brain membrane glycoprotein (SBMG). On 12 per cent sodium dodecylsulphate polyacrylamide gels this glycoprotein was shown to be a doublet with apparent molecular weights 24,000 and 25,000. By a number of physicochemical criteria SBMG was shown to have properties similar to those previously reported for Thy-1 isolated from other species. Immunological investigations, however, revealed that SBMG did not react with rabbit anti-rat Thy-1 and rabbit anti-SBMG did not recognise rat or chicken brain. By fluorescent antibody techniques the tissue distribution of SBMG appeared to be similar to that of Thy-1 in other species. A small population of peripheral blood and intestinal lymph lymphocytes were stained with anti-SBMG. These results suggest that sheep have an immunologically distinct Thy-1 homologue.
采用纯化Thy-1的标准方法处理羊脑,以纯化一种羊脑膜糖蛋白(SBMG)。在12%的十二烷基硫酸钠聚丙烯酰胺凝胶上,这种糖蛋白显示为一条双重带,表观分子量分别为24,000和25,000。根据多项物理化学标准,SBMG显示出与先前报道的从其他物种分离出的Thy-1相似的特性。然而,免疫学研究表明,SBMG不与兔抗大鼠Thy-1反应,兔抗SBMG也不能识别大鼠或鸡的脑。通过荧光抗体技术,SBMG的组织分布似乎与其他物种中Thy-1的分布相似。一小部分外周血和肠道淋巴淋巴细胞被抗SBMG染色。这些结果表明,绵羊具有一种免疫学上独特的Thy-1同源物。