Purification of a hybrid plasminogen activator protein |
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Authors: | J Deistung D M Forde J P O'Connell K A Proudfoot D Eaton F Willenbrock R O Kingaby B Hughes S Angal C Catterall |
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Institution: | Celltech Limited, Slough, Berks, U.K. |
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Abstract: | Recombinant DNA technology has been employed to produce a hybrid gene in which the kringle and serine protease domains of tissue plasminogen activator are linked to the heavy-chain Fd region of a fibrin-specific antibody. The hybrid gene is co-expressed with antibody light chains. This communication describes a purification procedure for the hybrid protein, involving affinity and ion-exchange chromatography. The purified hybrid protein has been used in vivo and in vitro clot lysis experiments and has been shown to be effective at clot dissolution. |
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