Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors.

@article{Hammond1987PrimarySO,
  title={Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors.},
  author={G. Hammond and C. L. Smith and I. Goping and D. Underhill and M. Harley and J. Reventós and N. Musto and G. Gunsalus and C. Bardin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1987},
  volume={84 15},
  pages={
          5153-7
        }
}
  • G. Hammond, C. L. Smith, +6 authors C. Bardin
  • Published 1987
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
We have isolated and sequenced cDNAs for corticosteroid binding globulin (CBG) prepared from human liver and lung mRNAs. Our results indicate that CBG mRNA is relatively abundant in the liver but is also present in the lung, testis, and kidney. The liver CBG cDNA contains an open reading frame for a 405-amino acid (Mr 45,149) polypeptide. This includes a predominantly hydrophobic, leader sequence of 22 residues that precedes the known NH2-terminal sequence of human CBG. We, therefore, predict… Expand
Molecular cloning and primary structure of rat thyroxine-binding globulin.
Molecular studies of corticosteroid binding globulin structure, biosynthesis and function
Substitutions of tryptophan residues in human corticosteroid-binding globulin: Impact on steroid binding and glycosylation
...
1
2
3
4
5
...