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- W2000692073 abstract "C1s, a subunit of the first component of complement was purified from human plasma using DEAE-cellulose column chromatography and hydroxylapatite column chromatography. The final product, purified 66-fold over the euglobulin fraction of plasma, was converted to C1 esterase by incubation with the C1r fraction or trypsin, although C1s was not activated on incubation alone for 2 h at 37 °C and pH 7.4. The homogeneity of the purified C1s preparation was confirmed with ultracentrifugation, disc electrophoresis and immunoelectrophoresis. Its s°20,w was 8.4 and its molecular weight was determined as 180 000 by gel filtration using Sephadex G-200. Comparison of the molecular weight of C1s with that of C1 esterase, which had been purified in our laboratory, suggested that the conversion of C1s to C1 esterase may be accompanied by a gross change of molecular weight due to removal of a peptide chain of mol. wt 60 000 to 70 000." @default.
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- W2000692073 date "1973-01-01" @default.
- W2000692073 modified "2023-09-27" @default.
- W2000692073 title "Purification of C1s, a subunit of the first component of complement from human plasma" @default.
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- W2000692073 doi "https://doi.org/10.1016/0005-2795(73)90092-5" @default.
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