Investigation on the substrate specificity of human plasmin using tripeptidyl-p-nitroanilide substrates
-
Add time:09/24/2019 Source:sciencedirect.com
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 B-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.
We also recommend Trading Suppliers and Manufacturers of D-PHE-VAL P-NITROANILIDE (cas 108321-89-7). Pls Click Website Link as below: cas 108321-89-7 suppliers
Prev:Identification of a new chromophoric substrate in the library of amino acid p-nitroanilides for continuous assay of VanX, a d,d-dipeptidase essential for vancomycin resistance
Next:Regular paperKinetic investigation of the hydrolysis of aminoacyl p-nitroanilides by dipeptidyl peptidase IV from human and pig kidney) - 【Back】【Close 】【Print】【Add to favorite 】
- Related Information
- A convenient synthesis of amino acid p-nitroanilides; synthons in the synthesis of protease substrates09/27/2019
- The action of Factor Xa on peptide p-nitroanilide substrates: substrate selectivity and examination of hydrolysis with different reaction conditions09/26/2019
- Regular paperKinetic investigation of the hydrolysis of aminoacyl p-nitroanilides by dipeptidyl peptidase IV from human and pig kidney09/25/2019
- Identification of a new chromophoric substrate in the library of amino acid p-nitroanilides for continuous assay of VanX, a d,d-dipeptidase essential for vancomycin resistance09/10/2019
- Mechanism of action and determination of the best substrate for a thrombin-like enzyme from Lachesis muta muta venom by regression analysis of the kinetic parameters determined with peptidyl p-nitroanilide substrates09/09/2019
- Kinetic properties of tripeptide lysyl chloromethyl ketone and lysyl p-nitroanilide derivatives towards trypsin-like serine proteinases09/08/2019
- PaperInvestigation of the substrate-binding site of human plasmin using tripeptidyl-p-nitroanilide substrates09/07/2019
- Polymer-assisted solution-phase parallel synthesis of dipeptide p-nitroanilides and dipeptide diphenyl phosphonates09/06/2019
- Steady-state kinetics of plasmin- and trypsin-catalysed hydrolysis of a number of tripeptide-p-nitroanilides09/05/2019


