Abstract
Bovine antiplasmin (antifibrinolysin) solutions with activities of 12–19 units/mg nitrogen have been obtained from bovine serum by 60% ammonium sulphate precipitation and isoelectric precipitation at pH 5.0 representing approximately a 6-fold purification of antiplasmin from serum. An additional 6.4-fold purification of antiplasmin was obtained by chromatography on a large diameter calcium phosphate gel column. Dialysis and lyophilization of the column eluate caused a 30% loss in activity. The dry antiplasmin was 25 times more potent than serum protein and was stable for 12 months when stored in a desiccator over P2O5 at −10°. Antiplasmin solutions with a specific activity twice that obtained with the large column could be eluted from a small diameter calcium phosphate column, but the activity decreased too rapidly to permit preparation of a lyophilized product.
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