PREPARATIVE PURIFICATION PROCESS FOR HUMAN FURIN

摘要

Recombinant truncated human furin was expressed in CHO cells and concentr ated approximately 50 -fold by ultrafiltration and diafiltration. The concen trate was purified by column chromatography on Capto-MMC~ resulting in a 30- 50 fold purification factor and a yield of at least 60%. The at least 20% pu re preparation obtained after Capto-MMC~ chromatography had already a purifi cation degree allowing on-column maturation of pro-VWF. Then an additional A rginine Sepharose chromatography purification was carried out. This two colu mn process for purification of truncated human furin resulted in an almost p ure furin preparation with a specific activity of approximately 290,000 U fu rin/mg protein and a yield of about 50%.