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• W2002976278 abstract "The rapidly acting inhibitor of plasminogen activators, PAI-1, was produced intracellularly in Saccharomyces cerevisiae by using the ADH2 promoter to drive the expression of the human PAI-1 cDNA. Approximately 8 mg of human PAI-1 was produced per liter of confluent yeast culture. A purification scheme which resulted in 20% recovery of isolated PAI-1 from the broken yeast cell homogenate was devised. Yeast-derived human PAI-1 differs from endothelial-type PAI-1 isolated from HT1080 fibrosarcoma cells in that the recombinant inhibitor does not contain carbohydrate side chains. Nevertheless, the activity and other functional attributes of yeast-derived PAI-1 are similar to those exhibited by HT1080 fibrosarcoma cell-derived PAI-1. Hence, this study demonstrates that expression of human PAI-1 in yeast is a viable strategy for the production of ample quantities of this key modulator of plasminogen activator-mediated proteolysis." @default.
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• W2002976278 date "1990-05-01" @default.
• W2002976278 modified "2023-09-23" @default.
• W2002976278 title "Purification and characterization of human plasminogen activator inhibitor type I expressed in Saccharomyces cerevisiae" @default.
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• W2002976278 doi "https://doi.org/10.1016/0003-9861(90)90286-8" @default.
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