tosylarginine-methyl-ester and valyl-leucyl-lysine-4-nitroanilide

tosylarginine-methyl-ester has been researched along with valyl-leucyl-lysine-4-nitroanilide* in 2 studies

Other Studies

2 other study(ies) available for tosylarginine-methyl-ester and valyl-leucyl-lysine-4-nitroanilide

Article	Year
Kinetic peculiarities of human tissue kallikrein: 1--substrate activation in the catalyzed hydrolysis of H-D-valyl-L-leucyl-L-arginine 4-nitroanilide and H-D-valyl-L-leucyl-L-lysine 4-nitroanilide; 2--substrate inhibition in the catalyzed hydrolysis of N Archives of biochemistry and biophysics, 2002, Apr-01, Volume: 400, Issue:1 Hydrolysis of D-valyl-L-leucyl-L-lysine 4-nitroanilide (1), D-valyl-L-leucyl-L-arginine 4-nitroanilide (2), and N alpha-p-tosyl-L-arginine methyl ester (3) by human tissue kallikrein was studied throughout a wide range of substrate concentrations. At low substrate concentrations, the hydrolysis followed Michaelis-Menten kinetics but, at higher substrate concentrations, a deviation from Michaelis-Menten behavior was observed. With the nitroanilides, a significant increase in hydrolysis rates was observed, while with the ester, a significant decrease in hydrolysis rates was observed. The results for substrates (1) and (3) can be accounted for by a model based on the hypothesis that a second substrate molecule binds to the ES complex to produce a more active or an inactive SES complex. The deviation observed for substrate (2) can be explained as a bimolecular reaction between the enzyme-substrate complex and a free substrate molecule. Topics: Catalysis; Chromogenic Compounds; Humans; Hydrolysis; Kallikreins; Kinetics; Models, Chemical; Oligopeptides; Protein Binding; Substrate Specificity; Tosylarginine Methyl Ester	2002
Influence of coagulation on the activation of plasminogen by streptokinase and urokinase. Thrombosis and haemostasis, 1979, Oct-31, Volume: 42, Issue:3 Human plasma was mixed with Ca++ or thrombin, and urokinase (UK) or streptokinase (SK) and a chromogenic substrate (S-2251: H-D-Val-Leu-Lys-pNA) specific to plasmin. The hydrolysis of S-2251 was higher when clot was formed by the addition of Ca++ or thrombin than in the absence of clot. The hydrolysis of S-2251 by euglobulin in the presence of UK was also higher when clot was formed, thus, inhibitors may not be related to the better activation of plasminogen, in the presence of fibrin clot. It may be suggested that plasminogen was better activated by activators (UK and SK) in the clot than in its absence. Topics: Blood Coagulation; Endopeptidases; Humans; Hydrolysis; Lysine; Oligopeptides; Plasminogen Activators; Serum Globulins; Streptokinase; Time Factors; Tosyl Compounds; Tosylarginine Methyl Ester; Urokinase-Type Plasminogen Activator	1979

Article

Year

Kinetic peculiarities of human tissue kallikrein: 1--substrate activation in the catalyzed hydrolysis of H-D-valyl-L-leucyl-L-arginine 4-nitroanilide and H-D-valyl-L-leucyl-L-lysine 4-nitroanilide; 2--substrate inhibition in the catalyzed hydrolysis of N

Archives of biochemistry and biophysics, 2002, Apr-01, Volume: 400, Issue:1

Hydrolysis of D-valyl-L-leucyl-L-lysine 4-nitroanilide (1), D-valyl-L-leucyl-L-arginine 4-nitroanilide (2), and N alpha-p-tosyl-L-arginine methyl ester (3) by human tissue kallikrein was studied throughout a wide range of substrate concentrations. At low substrate concentrations, the hydrolysis followed Michaelis-Menten kinetics but, at higher substrate concentrations, a deviation from Michaelis-Menten behavior was observed. With the nitroanilides, a significant increase in hydrolysis rates was observed, while with the ester, a significant decrease in hydrolysis rates was observed. The results for substrates (1) and (3) can be accounted for by a model based on the hypothesis that a second substrate molecule binds to the ES complex to produce a more active or an inactive SES complex. The deviation observed for substrate (2) can be explained as a bimolecular reaction between the enzyme-substrate complex and a free substrate molecule.

Topics: Catalysis; Chromogenic Compounds; Humans; Hydrolysis; Kallikreins; Kinetics; Models, Chemical; Oligopeptides; Protein Binding; Substrate Specificity; Tosylarginine Methyl Ester

2002

Influence of coagulation on the activation of plasminogen by streptokinase and urokinase.

Thrombosis and haemostasis, 1979, Oct-31, Volume: 42, Issue:3

Human plasma was mixed with Ca++ or thrombin, and urokinase (UK) or streptokinase (SK) and a chromogenic substrate (S-2251: H-D-Val-Leu-Lys-pNA) specific to plasmin. The hydrolysis of S-2251 was higher when clot was formed by the addition of Ca++ or thrombin than in the absence of clot. The hydrolysis of S-2251 by euglobulin in the presence of UK was also higher when clot was formed, thus, inhibitors may not be related to the better activation of plasminogen, in the presence of fibrin clot. It may be suggested that plasminogen was better activated by activators (UK and SK) in the clot than in its absence.

Topics: Blood Coagulation; Endopeptidases; Humans; Hydrolysis; Lysine; Oligopeptides; Plasminogen Activators; Serum Globulins; Streptokinase; Time Factors; Tosyl Compounds; Tosylarginine Methyl Ester; Urokinase-Type Plasminogen Activator

1979