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J. Biol. Chem., Vol. 258, Issue 1, 163-168, Jan, 1983
K Suzuki, J Nishioka and S Hashimoto
Protein C inhibitor was isolated from human plasma using conventional
chromatographic technique consisting of barium citrate adsorption,
polyethylene glycol fractionation, DEAE-Sepharose CL-6B treatment, ammonium
sulfate fractionation, dextran sulfate-agarose chromatography, gel
filtration on ACA-44, and DEAE-Sephacel chromatography. The purified
protein C inhibitor is a single polypeptide chain with an apparent Mr =
57,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The
inhibitor is heterogeneous in pI: six pIs exist between pH 7.4 and 8.6. The
inhibitor was shown to be different from the already known plasma protease
inhibitors by chemical and immunological analyses. It migrates to the late
alpha 1-globulin region on agarose gel electrophoresis. The inhibitor
reduced the amidolytic activity of activated protein C noncompetitively by
forming a 1:1 molar complex with the enzyme, determined by the use of a
fluorogenic substrate toward activated protein C (Boc-Leu-Ser-Thr-Arg-4-
methylcoumaryl-7-amide). The inhibition constant (Ki) of the inhibitor
against activated protein C was 5.8 x 10(-8) M. The inhibitor also blocked
the prolongation of activated partial thromboplastin time by activated
protein C. The immunoglobulin which was produced by the inhibitor
completely removed the inhibitory activity present in normal human plasma
against activated protein C. This suggests that the inhibitor which we have
isolated is the only inhibitor in plasma against activated protein C.
Protein C inhibitor. Purification from human plasma and characterization
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