Puchkova L V, Verbina I A, Denezhkina V V, Shavlovskiĭ M M, Gaĭtskoki V S, Neĭfakh S A
Biokhimiia. 1990 Dec;55(12):2182-9.
An electrophoretically pure preparation of ceruloplasmin (CP) receptor which retains its ability to bind to CP was isolated from human erythrocyte membranes. It was found that in terms of molecular mass, number and size of spontaneously proteolytic fragments as well as antigenicity, the CP receptor molecule strongly resembles that of CP. A comparative analysis of two-dimensional peptide maps of full tryptic digests of the both protein revealed that about 30% of CP peptides are identical in respect of their electrophoretic and chromatographic mobilities which points to the genetic independence of these proteins. The roles of CP and CP receptor in copper metabolism are discussed.
从人红细胞膜中分离出一种电泳纯的铜蓝蛋白(CP)受体制剂,该制剂保留了与CP结合的能力。研究发现,就分子量、自发蛋白水解片段的数量和大小以及抗原性而言,CP受体分子与CP分子极为相似。对这两种蛋白质的完整胰蛋白酶消化产物的二维肽图进行比较分析后发现,约30%的CP肽在电泳和色谱迁移率方面是相同的,这表明这些蛋白质在遗传上是独立的。文中还讨论了CP和CP受体在铜代谢中的作用。