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Affinity purification of plasma proteins: characterization of six affinity matrices and their application for the
M P te Booy1, W Riethorst, A Faber
1Dept. of Development and Quality Assurance, Netherlands Red Cross Blood Transfusion Service, Amsterdam.
Abstract:
For the purification of coagulation factor VIII, (1,1'-carbonyl-diimidazole [CDI]-activated) Sepharose CL-4B was functionalized with two aminoalkyl and four aminoalkyl-carbamylalkyl ligand-spacer combinations. The affinity matrices were contacted with human plasma. All affinity matrices showed complete adsorption of factor VIII (greater than 90%) and three aminoalkyl-carbamylalkyl Sepharoses gave factor-VIII recoveries of 50-65% and a factor-VIII preparation with a specific activity of 1-2 U factor VIII/mg of protein. Furthermore, no fibrinogen, immunoglobulin G and albumin could be detected in the isolated factor VIII. Optimal results were obtained using the di-methyl-aminopropyl-carbamyl-pentyl-Sepharose affinity matrix.