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• W1638703855 abstract "Human prothrombin cDNA has been expressed in mammalian cells to yield biologically active, fully gamma-carboxylated prothrombin. A 2.0-kilobase cDNA encoding full-length prothrombin was isolated from a human fetal liver library using a cDNA fragment recovered from a lambda gt11 human hepatoma expression library. Prothrombin cDNA was cloned into a mammalian expression vector and transfected into Chinese hamster ovary cells. Selection for expression of dihydrofolate reductase yielded cell lines secreting up to 0.55 microgram/ml of prothrombin. Recombinant prothrombin synthesized in the presence of vitamin K was quantitatively recovered from tissue culture medium by affinity chromatography using conformation-specific antibodies directed against the metal-stabilized, gamma-carboxylated conformer. The purified material migrated as a single band on denaturing polyacrylamide gels with an electrophoretic mobility equivalent to that of plasma-derived human prothrombin. Automated Edman degradation of recombinant prothrombin revealed a single amino-terminal sequence identical to that of plasma-derived prothrombin. Recombinant and plasma-derived prothrombin interacted similarly with antibodies specific for total prothrombin, abnormal des-gamma-carboxyprothrombin, and two metal-stabilized conformers of prothrombin. Recombinant prothrombin exhibited a specific coagulant activity equivalent to that of plasma-derived prothrombin. The gamma-carboxyglutamic acid analysis of recombinant prothrombin demonstrated 9.9 +/- 0.4 mol of gamma-carboxyglutamic acid/mol of prothrombin. These results represent the first description of the expression of a recombinant vitamin K-dependent protein in which all of the expressed protein is gamma-carboxylated." @default.
• W1638703855 created "2016-06-24" @default.
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• W1638703855 date "1987-05-01" @default.
• W1638703855 modified "2023-09-26" @default.
• W1638703855 title "Expression of completely gamma-carboxylated recombinant human prothrombin." @default.
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• W1638703855 doi "https://doi.org/10.1016/s0021-9258(18)48304-4" @default.
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