Expression and characterization of Kringle 1-4.5 domains of human plasminogen

Qing Wei Zhou, Jing Li Xie, Li Xin, Ren Xu, Qing Ye, Zai Ping Li, Ren Bao Gan

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The cDNA encoding Kringle 1-4 and part of Kringle 5 domains of human plasminogen (K1-4.5), obtained from HepG2 by RT-PCR, was cloned into expression vector pHIL-S1. The recombinant plasmid pHIL-K 1-4.5 was transformed into Pichia pastoris GS115 and the recombinant yeast was induced to express the recombinant proteins by methanol. The expressed proteins were purified by lysine affinity chromatography to a purity of 95%. The recombinant K1-4.5 inhibited the growth of bovine capillary endothelial cells (BAEC) stimulated by the basic fibroblast growth factor (bFGF), in a dosage-dependent manner with a half maximal concentration of 2 mg/L. rhK1-4.5 also inhibited 40% of the BAEC migration stimulated by bFGF in the concentration of 1 mg/L.

Original languageEnglish
Pages (from-to)138-142
Number of pages5
JournalActa Biochimica et Biophysica Sinica
Volume35
Issue number2
StatePublished - 2003

Keywords

  • Bioactivity
  • Expression
  • K1-4.5
  • Pichia pastoris
  • Purification

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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