A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S

• 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.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Medicinal Chemistry (hsv//eng)

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

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)