Peyriéras N, Louvard D, Jacob F
Proc Natl Acad Sci U S A. 1985 Dec;82(23):8067-71. doi: 10.1073/pnas.82.23.8067.
Uvomorulin is a cell surface glycoprotein involved in compaction of early mouse embryo. Antibodies, either monoclonal or polyclonal, raised against a purified tryptic fragment of uvomorulin recognize, in a detergent lysate of embryonal carcinoma cells metabolically labeled with 35S, three molecules (120, 100, and 88 kDa) that are not related, as judged by peptide mapping. Only the 120-kDa form is related to the tryptic fragment of uvomorulin and, thus, is considered as the native form of uvomorulin. Although all three products are apparently detectable at the cell surface, only the 120-kDa form is glycosylated. Coimmunoprecipitation of the three different polypeptides is probably due to shared epitopes rather than to their presence in a multimeric complex.
桥粒芯糖蛋白是一种参与早期小鼠胚胎致密化过程的细胞表面糖蛋白。针对桥粒芯糖蛋白纯化胰蛋白酶片段产生的单克隆或多克隆抗体，在经35S代谢标记的胚胎癌细胞去污剂裂解物中识别出三个分子（120、100和88 kDa），通过肽图谱分析判断，它们并无关联。只有120 kDa的形式与桥粒芯糖蛋白的胰蛋白酶片段相关，因此被视为桥粒芯糖蛋白的天然形式。尽管所有这三种产物在细胞表面似乎都可检测到，但只有120 kDa的形式进行了糖基化。这三种不同多肽的共免疫沉淀可能是由于共有表位，而非它们存在于多聚体复合物中。
