A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S |
| |
Authors: | S Gershagen P Fernlund A Lundwall |
| |
Affiliation: | Department of Clinical Chemistry, University of Lund, Malmö General Hospital, S-214 01 Malmö, Sweden |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|