On the specific interaction between the lysine-binding sites in plasmin and complementary sites in α2-antiplasmin and in fibrinogen
B Wiman, HR Lijnen, D Collen - … et Biophysica Acta (BBA)-Protein Structure, 1979 - Elsevier
Plasminogen and plasminogen derivatives which contain lysine-binding sites were found to
decrease the reaction rate between plasmin and α 2-antiplasmin by competing with plasmin
for the complementary site (s) in α 2-antiplasmin. The dissociation constant K d for the
interaction between intact plasminogen (Glu-plasminogen) and α 2-antiplasmin is 4.0 μM
but those for Lys-plasminogen or TLCK-plasmin are about 10-fold lower indicating a
stronger interaction. The lysine-binding site (s) which is situated in triple-loops 1–3 in the …
decrease the reaction rate between plasmin and α 2-antiplasmin by competing with plasmin
for the complementary site (s) in α 2-antiplasmin. The dissociation constant K d for the
interaction between intact plasminogen (Glu-plasminogen) and α 2-antiplasmin is 4.0 μM
but those for Lys-plasminogen or TLCK-plasmin are about 10-fold lower indicating a
stronger interaction. The lysine-binding site (s) which is situated in triple-loops 1–3 in the …