Fibrin binding. An essential property of anisoylated plasminogen streptokinase activator complex.
Use of an immobilised lysine column as a model system to assess the fibrin binding properties of plasminogen and its derivatives showed that anisoylated plasminogen streptokinase activator complex (APSAC) behaved in a manner similar to that of lys-plasminogen, the adsorption being inhibited in the presence of epsilon-aminocaproic acid. In 3 experimental systems using fibrin as the adsorbant, however, APSAC was more firmly bound than plasminogen and was not readily eluted by epsilon-aminocaproic acid.
Banton
C J
CJ
Biological Development Unit, Beecham Pharmaceuticals Research Division, Great Burgh, Epsom.
Overell
B G
BG
D016255:Anistreplase; D002851:Chromatography, High Pressure Liquid; D005337:Fibrin / Q000378:metabolism*; D005343:Fibrinolytic Agents / Q000378:metabolism*; D066298:In Vitro Techniques; D008239:Lysine / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D013300:Streptokinase / Q000378:metabolism*
D005343:Fibrinolytic Agents; D010446:Peptide Fragments; D016255:Anistreplase; D005337:Fibrin; D010958:Plasminogen; D013300:Streptokinase; D008239:Lysine