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Abstract
AbstractProtein C (PC), a plasma zymogen of a serine amidase with strong anticoagulant activity, has been purified to homogeneity as shown by sodium dodecyl sulfate electrophoresis. After isoelectric focusing in immobilized pH gradients, PC consists of six isobands, with isoelectric points (pI) between pH 4.8 and 5.1. That all the isobands were PC was confirmed by electroblotting on cellulose nitrate followed by immunoperoxidase staining. Activated PC gives a similar pattern of bands, with pIs ca. 0.5 units higher. Activated PC was also recognized by the monospecific antibody.
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