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Science 13 December 1991:
Vol. 254. no. 5038, pp. 1634 - 1636
DOI: 10.1126/science.1749935
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Articles

Science, Vol 254, Issue 5038, 1634-1636
Copyright © 1991 by American Association for the Advancement of Science

articles

Cloning and expression of the cDNA for human gamma-glutamyl carboxylase

SM Wu, WF Cheung, D Frazier, and DW Stafford

Department of Biology, University of North Carolina, Chapel Hill 27599-3280.

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.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)