title: Investigation on the substrate specificity of human plasmin using tripeptidyl-p-nitroanilide substrates.
abstract: The hydrolysis of 35 tripeptidyl-p-nitroanilides was studied with human plasmin and the kinetic parameters were determined. The individual contribution of the various side chains to the kinetic parameters was calculated by regression analysis. Considering Km, substrates having Z-D-Ile-Phe-Lys as well as H-D-Ile-Phe-Lys sequences were found to be the best, while Bz-Ile-Leu-Lys and pGlu-Leu-Lys sequences are the best for kcat. The Km values of substrates protected at N-terminus are lower, their kcat values are higher than those of the unprotected ones with the same sequence.
authors.forename: I
authors.initials: I
authors.lastname: Kiss
authors.forename: L
authors.initials: L
authors.lastname: Aurell
authors.forename: M
authors.initials: M
authors.lastname: Pozsgay
authors.forename: P
authors.initials: P
authors.lastname: Elödi
mesh_terms: D000595:Amino Acid Sequence; D000813:Anilides / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008968:Molecular Conformation; D012044:Regression Analysis; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D000813:Anilides; D005341:Fibrinolysin