Kinetic characteristics of fibrinogen and fibrin hydrolysis by plasmin 1 and 2 and miniplasmin.
Fibrinogen and fibrin hydrolysis by native plasmin 1 and 2 and by miniplasmin was studied. The degree of hydrolysis was estimated by the number of amino groups determined with trinitrobenzene sulphonic acid. The process was shown to obey Michaelis-Menten kinetics. Kinetic parameters of fibrinogen and fibrin hydrolysis by plasmin forms 1 and 2 were identical (KM = 6.5 X 10(-6) M, kcat = 7.1 sec-1) while for hydrolysis by miniplasmin KM = 20.0 X 10(-6) M, kcat = 3.58 sec-1. Thus, it was demonstrated that enzymatic properties of plasmin are to some extent dependent on the presence of lysine-binding sites. However, this appears not to have a decisive effect on fibrinolytic process.
D001665:Binding Sites; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005341:Fibrinolysin / Q000494:pharmacology*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008239:Lysine / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology*
D010446:Peptide Fragments; C019493:miniplasmin; D005337:Fibrin; D005340:Fibrinogen; D005341:Fibrinolysin; D008239:Lysine