Hybridization to an anti-activated platelet monoclonal antibody enhances fibrinolytic potency on urokinase.
The B-chain of urokinase (UK) was covalently linked by disulfide bond to the Fab fragment of an anti-human activated platelet monoclonal antibody (SZ-51). The UK-SZ-51 conjugate retained the original binding specificity of its parent antibody, and produced about a 5-fold enhancement in clot lysis in plasma over that of the urokinase in vitro. Whereas UK significantly decreased the concentration of fibrinogen in plasma clot assay supernatants, UK-SZ-51 did not.
Du
L
L
Department of Biochemistry, Nanjing University, PRC.
Yu
R R
RR
Hua
Z C
ZC
Zhu
D X
DX
Wu
G X
GX
Ruan
C G
CG
D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D015815:Cell Adhesion Molecules; D005342:Fibrinolysis / Q000187:drug effects*; D005343:Fibrinolytic Agents / Q000494:pharmacology; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000494:pharmacology; D000922:Immunotoxins / Q000494:pharmacology*; D014568:Urokinase-Type Plasminogen Activator / Q000494:pharmacology*
D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D015815:Cell Adhesion Molecules; D005343:Fibrinolytic Agents; D007140:Immunoglobulin Fab Fragments; D000922:Immunotoxins; D014568:Urokinase-Type Plasminogen Activator