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Cloning, Expression and Activity of Recombinant Human Angiostatin
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Abstract:
Objective: To express recombinant human angiostatin for further application in clinic. Methods: The complete encoding cDNA of human angiostatin was isolated from human embryo liver with RT PCR and expressed in secretory Pichia expression system. Recombinant human angiostatin was purified with heparin sepharose chromatography and its activity was determined in chick embryo chorioallantoic membrane (CAM) and wound healing assays. Results: Expressed in large quantity (yield=5 mg/L) and purified with heparin sepharose, recombinant angiostatin was showed to have a molecular weight of 43 kD in SDS PAGE and potently inhibit angiogenesis and wound healing. Conclusion: Recombinant human angiostatin was expressed efficiently in a biologically active form.
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