Abstract
Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage. The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated. The PEG precipitate (PEG-ppt) was separated by a Sephacryl S-200 column. Fractions were collected and those demonstrating maximum AT III antigen and progressive thrombin inhibition were pooled and reapplied to the washed Sephacryl S-200 column. Fractions were again collected and assayed via specific antisera for AT III, alpha 1-antitrypsin (alpha 1 AG), alpha 2-macroglobulin (alpha 2 M), and alpha 1-acid glycoprotein (alpha 1 AT). AT III antigen (AT III AGN) and progressive function were confined primarily to one peak containing virtually no alpha 2 M, a low level of alpha 1 AT, and moderate quantities of alpha 1 AG. The PEG-sup, PEG-ppt, AT III-HCF, and the fraction obtained after two passes across Sephacryl S-200 (S#2) were similar in that they showed reactivity with specific AT III antisera and demonstrated heparin cofactor activity. They differed, however, in that the PEG-sup and AT III-HCF demonstrated considerably reduced progressive antithrombin function as...Continue Reading
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