Gershagen S, Fernlund P, Lundwall A
FEBS Lett. 1987 Aug 10;220(1):129-35. doi: 10.1016/0014-5793(87)80890-6.
Affinity purified antibodies to human sex hormone binding globulin (SHBG) were used in screening a human liver cDNA library, constructed in the expression vector lambda gt11. One clone, identified as producing recombinant SHBG, carried a cDNA insert of 1.1 kb. The nucleotide sequence of the insert had an open reading frame coding for 356 amino acid residues. The coding sequence was followed by a short 3'-region of 19 non-translated nucleotides and a poly(A) tail. Confirmation that the cDNA clone represented human SHBG was obtained by the finding of a complete agreement in amino acid sequence with several peptide fragments generated from purified SHBG by proteolytic cleavage. The primary structure of SHBG shows a considerable homology to that of protein S, a vitamin K-dependent protein with functions in the coagulation system.
用人性激素结合球蛋白（SHBG）的亲和纯化抗体筛选构建于表达载体λgt11中的人肝脏cDNA文库。一个被鉴定为产生重组SHBG的克隆携带了一个1.1kb的cDNA插入片段。该插入片段的核苷酸序列有一个编码356个氨基酸残基的开放阅读框。编码序列后面是一段由19个非翻译核苷酸组成的短3'区域和一个多聚腺苷酸尾巴。通过发现cDNA克隆的氨基酸序列与通过蛋白水解切割从纯化的SHBG产生的几个肽片段完全一致，证实该cDNA克隆代表了人SHBG。SHBG的一级结构与蛋白S有相当大的同源性，蛋白S是一种维生素K依赖蛋白，在凝血系统中发挥作用。
