A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S
Författare
Summary, in English
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.
Avdelning/ar
Publiceringsår
1987
Språk
Engelska
Sidor
35-129
Publikation/Tidskrift/Serie
FEBS Letters
Volym
220
Issue
1
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Wiley-Blackwell
Ämne
- Medicinal Chemistry
Nyckelord
- Protein S
- Peptide Fragments/analysis
- Liver/analysis
- Humans
- Glycoproteins/analysis/*genetics
- DNA/*analysis
- Comparative Study
- Cattle
- *Base Sequence
- Amino Acid Sequence
- Animals
- Research Support
- Non-U.S. Gov't
- *Sequence Homology
- Nucleic Acid
- Sex Hormone-Binding Globulin/analysis/*genetics
Status
Published
Forskningsgrupp
- Clinical Chemistry, Malmö
ISBN/ISSN/Övrigt
- ISSN: 1873-3468