Mercer W R, Gogolin-Ewens K J, Lee C S, Brandon M R
Department of Veterinary Preclinical Sciences, University of Melbourne, Parkville, Victoria, Australia.
Placenta. 1989 Jan-Feb;10(1):71-82. doi: 10.1016/0143-4004(89)90008-8.
In order to elucidate the function of molecules of the ovine maternal-fetal interface a monoclonal antibody was produced to intact interplacentomal trophoblast membranes. Extensive immunohistological studies revealed that the monoclonal antibody recognizes a protein designated SBU-4 which originates in the intercaruncular regions of the gravid sheep uterus at about the time of implantation and increases in concentration throughout gestation. The data suggest that SBU-4 is produced by endometrial epithelial cells and that adjacent uninucleate cells of the trophoblast acquire the antigen by endocytosis. Initial biochemical analysis of the purified SBU-4 molecule prepared by monoclonal antibody immunoaffinity chromatography indicates that SBU-4 is high molecular weight glycoprotein complex comprising several sub-units.
为了阐明绵羊母胎界面分子的功能,制备了一种针对完整胎盘间滋养层细胞膜的单克隆抗体。广泛的免疫组织学研究表明,该单克隆抗体识别一种名为SBU-4的蛋白质,它大约在着床时起源于妊娠绵羊子宫的肉阜间区域,并在整个妊娠期浓度增加。数据表明,SBU-4由子宫内膜上皮细胞产生,相邻的滋养层单核细胞通过内吞作用获得该抗原。通过单克隆抗体免疫亲和层析制备的纯化SBU-4分子的初步生化分析表明,SBU-4是一种由几个亚基组成的高分子量糖蛋白复合物。