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• W2004133690 abstract "Recombinant human protein C (rhPC) secreted in the milk of transgenic pigs was studied. Transgenes having different regulatory elements of the murine milk protein, whey acidic protein, were used with cDNA and genomic human protein C (hPC) DNA sequences to obtain lower and higher expressing animals. The cDNA pigs had a range of expression of about 0.1–0.5 g/l milk. Two different genomic hPC pig lines have expressed 0.3 and 1–2 g/l, respectively. The rhPC was first purified at yields greater than 60 per cent using a monoclonal antibody (mAb) to the activation site on the heavy chain of hPC. Subsequent immunopurification with a calcium-dependent mAb directed to the γ-carboxyglutamic acid domain of the light chain of hPC was used to fractionate a population having a higher specific anticoagulant activity in vitro. The higher percentages of Ca2+-dependent conformers isolated from the total rhPC by immunopurification correlated well with higher specific activity and lower expression. A rate limitation in γ-carboxylation of rhPC was clearly identified for the higher expressing animals. Thus, transgenic animals with high expression levels of complex recombinant proteins produced a lower percentage of biologically active protein." @default.
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• W2004133690 date "1996-10-01" @default.
• W2004133690 modified "2023-09-30" @default.
• W2004133690 title "Affinity purification of biologically active and inactive forms of recombinant human protein C produced in porcine mammary gland" @default.
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• W2004133690 doi "https://doi.org/10.1002/(sici)1099-1352(199634/12)9:5/6<407::aid-jmr277>3.0.co;2-x" @default.
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