Expression, Purification, and Characterization of Prothrombin Kringle 2

Tai Youn Rhim, Eunkyung Kim, Chan Soo Park, Soung Soo Kim

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Previously, we reported that the prothrombin kringle 2 (fragment 2), induced by LPS administration into rabbit, inhibited bFGF-stimulated BCE cell growth (Lee et al., 1998). In this study, we cloned and overexpressed the kringle 2 domain of rabbit and human prothrombin as a fusion protein with the pelB leader sequence in E. coli using the T7 promoter. The fusion protein was cleaved during translocation into the periplasmic space, and cleaved recombinant protein was readily isolated from whole cell lysate by DEAE-Sepharose and Sephacryl S-200 gel filtration chromatography. Both the recombinant rabbit and human prothrombin kringle 2 showed very similar biochemical and functional characteristics to the rabbit prothrombin kringle 2 purified from rabbit serum, in terms of abnormal electrophoretic migration and endothelial cell growth inhibitory activity.

Original languageEnglish
Pages (from-to)147-153
Number of pages7
JournalJournal of biochemistry and molecular biology
Issue number2
Publication statusPublished - 1999 Mar 31

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Expression, Purification, and Characterization of Prothrombin Kringle 2'. Together they form a unique fingerprint.

Cite this