Glycosylated and nonglycosylated forms of PAI-1 were separated from HepG 2 cell by immunoaffinity chromatography with anti-PAI-1 monoclonal antibody, and the recombinant PAI-1 were purified from the media of expressed bacteria line of pYZhBI-66. Some functions and characteristics of the three PAI-1 were compared, such as the inhibiting effect on tPA, the activation by denaturation, the stability to thermal or pH changes, and the activation by fibrinogen and heparin. The results emphasized the roles of the oligosaccharide.
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