Dissociation constant of protonization of fumaric and maleic acids in acid medium

1968 ◽  
Vol 33 (2) ◽  
pp. 594-596 ◽  
Author(s):  
L. Pospíšil ◽  
J. Tomanová ◽  
J. Kůta
Keyword(s):  
Dissociation Constant ◽  
Acid Medium

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

The Binding of Calcium Ions to Bovine Factor X by Rate Dialysis

1978 ◽  
Vol 40 (02) ◽  
pp. 350-357
Author(s):  
Robert H Yue ◽  
Menard M Gertler
Keyword(s):  
Molecular Weight ◽  
Dissociation Constant ◽  
Calcium Ions ◽  
Activation Process ◽  
Factor X ◽  
The Real ◽  
High Affinity ◽  
Binding Data ◽  
Sequential Mechanism ◽  
Bovine Factor

SummaryThe binding of Ca+2 to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of 45Ca+2. The binding data are consistent with a model of sequential mechanism. One mole of Ca+2 binds to the glycoprotein with a dissociation constant of 5.2 × 10-5 M and an additional 39 ± 4 moles of Ca+2 bind to this zymogen with a dissociation constant of 3.7 × 10-3M. The binding of the high affinity Ca+2 causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell’s viper venom.

Kinetics and Mechanism of Oxidation of Paracetamol by Thallic Perchlorate in Acid Medium

2015 ◽  
Vol 4 (3) ◽  
pp. 302-309 ◽  
Author(s):  
Deepmala Pareek ◽  
Riya Sailani ◽  
Vinita Gupta ◽  
Chandra Khandelwal ◽  
Prem Sharma
Keyword(s):  
Acid Medium ◽  
Kinetics And Mechanism ◽  
Mechanism Of Oxidation

CORROSION INHIBITION OF ZINC IN HYDROCHLORIC ACID MEDIUM USING UREA INHIBITOR

2007 ◽  
Vol 10 (2) ◽  
pp. 31-38 ◽  
Author(s):  
Khulood AL-Saadie ◽  
◽  
Nadia Abdul Karime ◽  
Israa M Al-Mousawi ◽  
◽  
...  
Keyword(s):  
Hydrochloric Acid ◽  
Acid Medium ◽  
Corrosion Inhibition ◽  
Hydrochloric Acid Medium
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