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Human protein C was purified. and the mechanism of action of activated protein C as an anticoagulant in plasma was studied. Protein C was purified from commercial factor IX concentrate by DEAE-Sephadex and dextran sulfate-Sepharose chromatography and preparative polyacrylamide gel electrophoresis. Purified protein C appeared homogenous at 62.000 mol wt on nonreduced SDS-polyacrylamide gels and. following reduction. protein C gave two polypeptide chains of 40.000 and 22.000 mol wt. Protein
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Marlar et al. (1982) studied this question.
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