An improved method for removal of antithrombin III from post-heparin plasma lipase fractions with a high recovery rate.

TL;DRAbstract

Affinity chromatography on heparin-Sepharose has been widely used for the purification of post-heparin plasma triglyceride lipases, but this procedure alone yields lipase fractions with a high content of antithrombin III (AT), which also binds to heparin and coelutes with the lipases. A rapid procedure in which this major contaminant is reduced by the use of affinity chromatography on heparin-Sepharose with low affinity for AT and further removal by anti-AT IgG Affi-Gel 10 column chromatography is reported and the results are compared with these of the conventional heparin-Sepharose and Concanavalin A-Sepharose column chromatography two step method. While the AT contamination of hepatic lipase eluate from conventional heparin-Sepharose column chromatography was 92 mg/dl in 100 mg/dl protein, heparin-Sepharose with low affinity for AT yielded samples with 55 mg/dl in 100 mg/dl protein. A second passage on concanavalin A-Sepharose of the sample from conventional heparin-Sepharose reduced

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