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- W2368743664 abstract "Aim To purify a long half-life tPA combination mutant,which was deglycosylated from K1 and K2 domain,deleted PAI-1 binding site(residues Lys296 to Gly302) and designated as FrGGI.Methods The FrGGI was highlevel stable expressed in CHO cell through coamplification of the mutant and DHFR cDNA. The mutant protein was purified by Lysine sepharose 4B and Zn 2+ sepharose 4B affinity chromotography from the culture supernatant after 24 hours incubation.Result We have purified the FrGGI protein, it has high specific activity.This will make possible its biological analyses and application.Conclusion TPA and its mutants with K2 domain can be purified effectively using Lysine sepharose 4B and Zn 2+ sepharose 4B affinity chromotography." @default.
- W2368743664 created "2016-06-24" @default.
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- W2368743664 date "2000-01-01" @default.
- W2368743664 modified "2023-09-23" @default.
- W2368743664 title "Purification of a combination mutant(FrGGI) of human tissue-type plasminogen activator(t-PA) from the culture medium of the expression cell" @default.
- W2368743664 hasPublicationYear "2000" @default.
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