A Procedure for Isolation of Human Protein C and Protein S as by-Products of the Purification of Factors VII, IX, X and Prothrombin
- 1 September 1983
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 13 (3), 191-214
- https://doi.org/10.1080/00327488308064248
Abstract
A DEAE-Sephadex column chromatography step utilized to purify human Factor VII consistently yields a protein peak between the factor VII activity peak and prothrombin, factor X and factor IX activity peak (S.P. Bajaj, S.I. Rapaport, and S.F. Brown: J. Biol. Chem. 251., 253-259, 1981). We now report that this protein peak contains protein C and protein S. Preparative disc polyacryla-mide gel electrophoresis of the proteins in this peak 'permitted a complete separation of protein C from protein S. Protein C at this step usually contained approximately 5-10% of Factor X, which could be removed by a goat anti-human Factor X antibody column. For a typical preparation, starting with 10L of plasma, the yield of Protein C was 5 mg and of protein S was 4 mg. Both proteinsThis publication has 19 references indexed in Scilit:
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