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. 1986 Jan 1;41(1):89-98.
doi: 10.1016/0049-3848(86)90282-3.

Purification of human factor XII from plasma using zinc chelate affinity chromatography

Purification of human factor XII from plasma using zinc chelate affinity chromatography

R A Pixley et al. Thromb Res. .

Abstract

Human factor XII (Hageman Factor) was isolated from human plasma to apparent homogeneity using a four step procedure with yields up to 30%. The method, which is more rapid than the current conventional procedures, consists of a 25-50% ammonium sulfate fractionation, two affinity chromatography steps using Zinc Chelate Sepharose, followed by gel filtration. The isolated zymogen factor XII was a single protein component when examined by SDS PAGE with a Mr of 80,000. Activation of zymogen factor XII to its active enzymatic forms by kallikrein resulted in factor XIIa and factor XIIf as observed with factor XII purified by other procedures.

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