[The hydrolysis of Glu(gamma-epsilon)Lys-amide bonds in D-dimer fragment of fibrin by destabilase from medicinal leech].
A study was made of the dependence of the hydrolysis rate of isopeptide bonds in the D-dimer, the product of limited proteolysis of the stabilized fibrin by plasmin, on the high-molecular substrate concentration catalyzed by destabilase from the medicinal leech. The formation of the reaction product was electrophoretically measured by the increase in the quantity of D-monomer. This dependence was shown to be nonlinear.
Baskova
I P
IP
Biological Faculty, Moscow State University, Russia. leech@humgen.siobc.ras.ru
Zavalova
L L
LL
Basanova
A V
AV
Grigor'eva
O V
OV
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D007865:Leeches / Q000201:enzymology; D013379:Substrate Specificity
D005338:Fibrin Fibrinogen Degradation Products; C036309:fibrin fragment D; D010450:Endopeptidases; C045348:fibrin destabilase