隔离和序列分析的变体形式的人类钴胺传递蛋白II。
文章的细节
-
引用
复制到剪贴板 -
李N, Seetharam年代,林德曼J, Alpers DH, Arwert F, Seetharam B
隔离和序列分析的变体形式的人类钴胺传递蛋白II。
Biochim Biophys学报。1993年2月20日,1172 (2):21 - 30。
- PubMed ID
-
8439564 (在PubMed]
- 文摘
-
两个cDNA克隆(分别为1.9 kb和1.5 kb)编码完整人类TC II已经从人类内皮细胞分离cDNA图书馆和测序。两个克隆之间的差异的长度5 '端和3 '端非编码区和密码子198年和219年的位置。最近克隆不同于孤立的(人类内皮细胞)的互补为TC II (Platica, O。Janecko, R。Quadros,那么Regee,。,罗曼·r·罗斯伯格,……(1991)生物。化学。266年,7860 - 7863)在密码子259年和376年,计算π值。体外转录翻译紧随其后在网织红细胞溶解产物体系,sds - page显示43 kDa的孤立cDNA克隆编码一种蛋白质。犬治疗胰腺癌微粒体,分子质量的体外翻译产品是减少到41.5 kDa,指示一个大约1.5 kDa信号肽的存在。这个翻译产品与兔免疫沉淀反应anti-serum人类TC二世和能够绑定到Cbl-Sepharose珠子。TC二世的氨基酸序列比对与其他Cbl结合蛋白(人类钴胺传递蛋白鼠内在因素,我和猪haptocorrin)显示只有33%的同源性。 However, there were four regions of greater than 80% homology and two regions of about 60% homology. These regions encompass the majority of the hydrophobic areas of the Cbl-binders. Based on these studies, we suggest that structural basis for the expression of different polymorphic forms of TC II may be due to single point mutations and that TC II, like other mammalian Cbl-binders, have evolved from a common ancestral gene. Furthermore, the Cbl-binding functional domain most probably resides in a hydrophobic pocket which is formed by all or some of the six regions of high homology.