Micellar effect on the kinetics of the base equilibrium of amino acids studied by the ultrasonic absorption method

1991 ◽  
Vol 87 (12) ◽  
pp. 1857 ◽  
Author(s):  
Teruyo Yamashita ◽  
Kazue Tanaka ◽  
Hiroshige Yano ◽  
Shoji Harada
Keyword(s):  
Amino Acids ◽  
Ultrasonic Absorption ◽  
Absorption Method ◽  
Base Equilibrium ◽  
Kinetics Of ◽  
Micellar Effect

Micellar Catalytic Effects on the Kinetics of the Ionization of Basic Amino Acid and Acidic Amino Acid Studied by the Ultrasonic Absorption Method

Langmuir ◽  
1995 ◽  
Vol 11 (5) ◽  
pp. 1477-1481
Author(s):  
Teruyo Yamashita ◽  
Miyuki Yamasaki ◽  
Takayuki Sano ◽  
Shoji Harada ◽  
Hiroshige Yano
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Ultrasonic Absorption ◽  
Absorption Method ◽  
Acidic Amino Acid ◽  
Kinetics Of ◽  
Catalytic Effects

Micellar effects on the kinetics of the hydrolysis of alkylamines studied by the ultrasonic absorption method

1984 ◽  
Vol 88 (12) ◽  
pp. 2671-2674 ◽  
Author(s):  
Teruyo Yamashita ◽  
Hiroshige Yano ◽  
Shoji Harada ◽  
Tatsuya Yasunaga
Keyword(s):  
Ultrasonic Absorption ◽  
Absorption Method ◽  
Micellar Effects ◽  
Kinetics Of ◽  
Hydrolysis Of

Micellar effects on the kinetics of the protolysis of carboxylic acids studied by the ultrasonic absorption method

1984 ◽  
Vol 88 (22) ◽  
pp. 5406-5409 ◽  
Author(s):  
Shoji Harada ◽  
Teruyo Yamashita ◽  
Hiroshige Yano ◽  
Naoki Haga ◽  
Tatsuya Yasunaga
Keyword(s):  
Carboxylic Acids ◽  
Ultrasonic Absorption ◽  
Absorption Method ◽  
Micellar Effects ◽  
Kinetics Of

The Kinetics of Inhibition of the Action of Thrombin by the Fibrinopeptides Formed during the Clotting of Fibrinogen

1966 ◽  
Vol 16 (01/02) ◽  
pp. 277-295 ◽  
Author(s):  
A Silver ◽  
M Murray
Keyword(s):  
Amino Acids ◽  
Competitive Inhibition ◽  
Amorphous Material ◽  
Peptide Bond ◽  
Initial Reaction ◽  
Reaction Products ◽  
Coagulation Mechanism ◽  
Kinetics Of ◽  
Kinetics Of Inhibition ◽  
Burk Plot

SummaryVarious investigators have separated the coagulation products formed when fibrinogen is clotted with thrombin and identified fibrinopeptides A and B. Two other peaks are observed in the chromatogram of the products of coagulation, but these have mostly been dismissed by other workers. They have been identified by us as amino acids, smaller peptides and amorphous material (37). We have re-chromatographed these peaks and identified several amino acids. In a closed system of fibrinogen and thrombin, the only reaction products should be fibrin and peptide A and peptide B. This reasoning has come about because thrombin has been reported to be specific for the glycyl-arginyl peptide bond. It is suggested that thrombin also breaks other peptide linkages and the Peptide A and Peptide B are attacked by thrombin to yield proteolytic products. Thrombin is therefore probably not specific for the glycyl-arginyl bond but will react on other linkages as well.If the aforementioned is correct then the fibrinopeptides A and B would cause an inhibition with the coagulation mechanism itself. We have shown that an inhibition does occur. We suggest that there is an autoinhibition to the clotting mechanism that might be a control mechanism in the human body.The experiment was designed for coagulation to occur under controlled conditions of temperature and time. Purified reactants were used. We assembled an apparatus to record visually the speed of the initial reaction, the rate of the reaction, and the density of the final clot formed after a specific time.The figures we derived made available to us data whereby we could calculate and plot the information to show the mechanism and suggest that such an inhibition does exist and also further suggest that it might be competitive.In order to prove true competitive inhibition it is necessary to fulfill the criteria of the Lineweaver-Burk plot. This has been done. We have also satisfied other criteria of Dixon (29) and Bergman (31) that suggest true competitive inhibition.

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