1. Cloning and Expression of the cDNA for Human γ-glutamyl Carboxylase
- Author
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Darrel W. Stafford, Wing-Fai Cheung, Sheue Mei Wu, and Dan Frazier
- Subjects
Molecular Sequence Data ,Biology ,Polymerase Chain Reaction ,Gamma-glutamyl carboxylase ,Ligases ,Complementary DNA ,Animals ,Humans ,Amino Acid Sequence ,Cloning, Molecular ,Integral membrane protein ,Cloning ,chemistry.chemical_classification ,Multidisciplinary ,Base Sequence ,DNA ,Transfection ,Molecular biology ,Recombinant Proteins ,Pyruvate carboxylase ,Transmembrane domain ,Enzyme ,Carbon-Carbon Ligases ,Oligodeoxyribonucleotides ,Biochemistry ,chemistry ,Cattle ,Sequence Alignment - Abstract
The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.
- Published
- 1991
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