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

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Author

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.

Publishing year

1987

Language

English

Pages

35-129

Publication/Series

FEBS Letters

Volume

220

Issue

1

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Medicinal Chemistry

Keywords

  • 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

Research group

  • Clinical Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1873-3468