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- W934710804 abstract "This chapter presents the procedure for purification of α2-Antiplasmin. α2-antiplasmin has been shown to interact weakly with the lysinebinding sites in plasminogen. This can be used for affinity chromatographic purification of the inhibitor, and if followed by DEAESephadex and concanavalin A-Sepharose chromatography, a pure α2-antiplasmin preparation is obtained in good yield (30- 40%). Alternatively, affinity chromatography can be carried out on a fragment from plasminogen containing the three NH2-terminal triple-loop structures coupled to Sepharose. The material obtained from this step is already 80-90% pure, and the major contaminant, fibrinogen or highmolecular- weight fibrinogen-degradation products, are easily removed by gel filtration on Ultrogel AcA 44. Several procedures for measuring α2-antiplasmin activity are also described. They all measure a decrease in plasmin activity after addition of an α2-antiplasmin sample to a specified amount of plasmin, using either synthetic substrates or clot-lysis methods. Procedures using the synthetic-peptide substrate D-Val-Leu-Lys-Nan are most frequently and conveniently used." @default.
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- W934710804 date "1981-01-01" @default.
- W934710804 modified "2023-09-28" @default.
- W934710804 title "[32] Human α2-antiplasmin" @default.
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- W934710804 doi "https://doi.org/10.1016/s0076-6879(81)80034-1" @default.
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