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. 1997 May 5;185(9):1595–1604. doi: 10.1084/jem.185.9.1595

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Purification of recombinant MDC from CHO cells. A PCR fragment containing bases 1–403 of the MDC cDNA was subcloned into a mammalian expression vector driven by the CMV promoter and transfected into CHO cells. Culture supernatant from an individual transfected clone was harvested 4 d after cells reached confluency. MDC in the media was concentrated and purified by binding to a heparin-Sepharose column in 0.35 M NaCl. The left panel shows the column chromatogram. Fractions collected were flowthrough (FT), 0.35 M NaCl wash (A), 0.7 M NaCl elution (B), repeat of 0.7 M NaCl elution (C), and 1.5 M NaCl elution (D). The right panel shows SDS-PAGE analysis (18% Tris glycine) of the supernatant loaded onto the column (L) and fractions FT, B, C, and D. MDC eluted in fraction B (arrow). The gel was transferred to polyvinylidene difluoride membrane, and the MDC band was excised for NH₂-terminal sequencing.