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Renaturation and purification of recombinant tissue‐type plasminogen activator expressed in E. coli
Author(s) -
Hua ZiChun
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201851
Subject(s) - recombinant dna , plasminogen activator , microbiology and biotechnology , chemistry , biochemistry , biology , gene , genetics
Under the control of trp promoter, human tissue‐type plasminogen activator was expressed in E. coil in the form of inclusion body. The recombinant t‐PA was recovered for renaturation from preparative native PAGE gel by zinc acetate staining and electroelution. After renaturation in vitro, the recombinant t‐PA was purified by benzamidine affinity chromatography and lysine affinity chromatography. The purified t‐PA showed homogeneous on silver‐stained SDS‐PAGE gel, with a specific activity of 240,000I.U./mg protein.