A cDNA coding for human sex hormone binding globulin Homology to vitamin K-dependent protein S
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 λgt 11. 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.
- Publication:
-
FEBS Letters
- Pub Date:
- January 1987
- DOI:
- 10.1016/0014-5793(87)80890-6
- Bibcode:
- 1987FEBSL.220..129G
- Keywords:
-
- Sex hormone binding globulin;
- Sex hormone;
- Carrier protein;
- Plasma protein;
- Blood coagulation