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  • Title: Expression and characterization of recombinant human micro-plasminogen.
    Author: Ma Z, Lu W, Wu S, Chen J, Sun Z, Liu JN.
    Journal: Biotechnol Lett; 2007 Apr; 29(4):517-23. PubMed ID: 17206368.
    Abstract:
    Micro-plasminogen (microPlg) gene amplified from human liver cells by reverse transcription PCR was inserted into expression vector pET-28a (pET-28a/microPlg) and transformed into E. coli strain BL21(DE3). Recombinant human micro-plasminogen (rh-microPlg) was over-expressed as inclusion bodies when induced with IPTG. After renaturation and purification, 16 mg rh-microPlg/l was obtained with a homogeneity of 95% (w/w). Pro-urokinase (proUK)-induced rh-microPlg activation was significantly faster than when Glu-plasminogen was the substrate. The catalytic efficiency of urokinase (UK) activation of rh-microPlg was twice that of Glu-plasminogen. While recombinant human micro-plasmin (rh-microPlm) and Lys-plasmin had a similar amidolytic activity against a small substrate, D-valyl-L-leucyllysine-p-nitroaniline dihydrochloride, Lys-plasmin activated proUK with a catalytic efficiency about fourfold greater than did rh-microPlm. These results suggested that the kringle 1-5 domain of plasminogen and plasmin may modify both UK activation of plasminogen and plasmin activation of proUK, respectively.
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