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

Gershagen, S.; Fernlund, Per LU and Lundwall, Åke LU (1987) In FEBS Lett 220(1). p.129-35
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... (More)
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. (Less)
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published
subject
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
in
FEBS Lett
volume
220
issue
1
pages
129 - 35
publisher
Elsevier
external identifiers
  • Scopus:0023273737
language
English
LU publication?
no
id
e85083db-805b-4366-bba0-07c67b230da7 (old id 3965145)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2956126
date added to LUP
2013-08-11 14:25:24
date last changed
2016-06-29 09:05:36
@misc{e85083db-805b-4366-bba0-07c67b230da7,
  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.},
  author       = {Gershagen, S. and Fernlund, Per and Lundwall, Åke},
  keyword      = {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},
  language     = {eng},
  number       = {1},
  pages        = {129--35},
  publisher    = {ARRAY(0xa379ce0)},
  series       = {FEBS Lett},
  title        = {A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S},
  volume       = {220},
  year         = {1987},
}