Purification of human prothrombin fragment 1 using hydrophobic interaction chromatography on phenyl-sepharose.
Hydrophobic interaction chromatography on Phenyl-Sepharose for the purification of prothrombin fragment 1 is described. The results suggest that this method is both easier and more effective than the use of anion-exchange chromatography for the purification of fragment 1. In addition, the results presented here suggest that prothrombin has rather extensive hydrophobic properties.
D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D010446:Peptide Fragments / Q000302:isolation & purification*; D011498:Protein Precursors; D011516:Prothrombin / Q000302:isolation & purification*; D012685:Sepharose / Q000031:analogs & derivatives; D012967:Sodium Dodecyl Sulfate
D010446:Peptide Fragments; D011498:Protein Precursors; D012967:Sodium Dodecyl Sulfate; C020927:phenyl-sepharose; C029733:prothrombin fragment 1; D011516:Prothrombin; D012685:Sepharose