Purification of a hybrid plasminogen activator protein.
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.
Deistung
J
J
Celltech Limited, Slough, Berks, U.K.
Forde
D M
DM
O'Connell
J P
JP
Proudfoot
K A
KA
Eaton
D
D
Willenbrock
F
F
Kingaby
R O
RO
Hughes
B
B
Angal
S
S
Catterall
C
C
D000818:Animals; D001777:Blood Coagulation; D002478:Cells, Cultured; D002846:Chromatography, Affinity / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D006224:Cricetinae; D003412:Cricetulus; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005337:Fibrin / Q000276:immunology; D006824:Hybridization, Genetic / Q000235:genetics*; D010053:Ovary / Q000737:chemistry / Q000166:cytology; D011995:Recombination, Genetic; D010959:Tissue Plasminogen Activator / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*
D005337:Fibrin; D010959:Tissue Plasminogen Activator