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  • Title: Characterization and novel purification of recombinant human protein C from three mammalian cell lines.
    Author: Yan SC, Razzano P, Chao YB, Walls JD, Berg DT, McClure DB, Grinnell BW.
    Journal: Biotechnology (N Y); 1990 Jul; 8(7):655-61. PubMed ID: 1366628.
    Abstract:
    Human Protein C (HPC), an antithrombotic factor with potential clinical utility, is a vitamin K-dependent protein that has several complex post-translational modifications. In an effort to define the functional roles of these modifications, recombinant HPC (rHPC) was expressed in and characterized from 3 adenovirus-transformed cell lines. The rHPC in crude culture medium from the 3 cell lines displayed anticoagulant activities that were either higher, slightly lower or much lower than that of plasma HPC. The rHPC from each cell line was purified and characterized using a novel, but simple chromatographic method, termed "pseudo-affinity", capable of resolving molecules differing by only very slight modifications. We demonstrate the critical dependence of full gamma-carboxylation on the function of this protein. In addition, our data indicate that both the gamma-carboxyglutamate and glycosyl contents affect the functional activities of rHPC.
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