Application of the median method to estimate the kinetic constants of the substrate uncompetitive inhibition equation

2017 ◽  
Vol 418 ◽  
pp. 122-128 ◽  
Author(s):  
Pedro L. Valencia ◽  
Carolina Astudillo-Castro ◽  
Diego Gajardo ◽  
Sebastián Flores
Keyword(s):  
Kinetic Constants ◽  
Uncompetitive Inhibition

KINETIC CONSTANTS DETERMINATION OF PETROLEUM REFINERY EFFLUENT TREATMENT IN A UASB REACTOR USING RSM

2017 ◽  
Vol 16 (1) ◽  
pp. 121-130 ◽  
Author(s):  
Seyyed Mohammad Mousavi ◽  
Seyed Omid Rastegar ◽  
Seyed Abbas Shojaosadati ◽  
Soheila Sheibani
Keyword(s):  
Petroleum Refinery ◽  
Kinetic Constants ◽  
Effluent Treatment ◽  
Uasb Reactor ◽  
Refinery Effluent ◽  
Petroleum Refinery Effluent

Supersaturation of solutions in crystallisers with the well stirred suspension

1980 ◽  
Vol 45 (7) ◽  
pp. 1920-1927 ◽  
Author(s):  
Jaroslav Nývlt
Keyword(s):  
High Accuracy ◽  
Nucleation And Growth ◽  
Kinetic Constants ◽  
Derived Relations ◽  
Metastable Region ◽  
The Given

Relations were derived comparing the steady supersaturation in the continuous MSMPR and/or bath crystallisers with the stirred suspension having the maximum supersaturation corresponding to the boundary of metastable region at the given conditions. The derived relations include only the quantities used for the system constant BN from the corresponding crystallisation experiments. By use of supersaturation in the crystalliser obtained by the described method it is possible to evaluate the kinetic constants of nucleation and growth. However, it is not possible to expect a high accuracy of the data so obtained.

Kinetics and mechanism of the reaction of iron(III) with 6-methyl-2,4-heptanedione and 3,5-heptanedione

1990 ◽  
Vol 55 (8) ◽  
pp. 1984-1990 ◽  
Author(s):  
José M. Hernando ◽  
Olimpio Montero ◽  
Carlos Blanco
Keyword(s):  
Aqueous Solution ◽  
Metal Ion ◽  
Activation Parameters ◽  
Enol Form ◽  
Kinetics And Mechanism ◽  
Kinetic Constants ◽  
Steric Factors ◽  
Kinetics Of ◽  
Mechanism Of The Reaction

The kinetics of the reactions of iron(III) with 6-methyl-2,4-heptanedione and 3,5-heptanedione to form the corresponding monocomplexes have been studied spectrophotometrically in the range 5 °C to 16 °C at I 25 mol l-1 in aqueous solution. In the proposed mechanism for the two complexes, the enol form reacts with the metal ion by parallel acid-independent and inverse-acid paths. The kinetic constants for both pathways have been calculated at five temperatures. Activation parameters have also been calculated. The results are consistent with an associative activation for Fe(H2O)63+ and dissociative activation for Fe(H2O)5(OH)2+. The differences in the results for the complexes of heptanediones studied are interpreted in terms of steric factors.

scholarly journals Simulation of extracellular nucleotide hydrolysis and determination of kinetic constants for the ectonucleotidases.

1986 ◽  
Vol 261 (33) ◽  
pp. 15505-15507
Author(s):  
L L Slakey ◽  
K Cosimini ◽  
J P Earls ◽  
C Thomas ◽  
E L Gordon
Keyword(s):  
Kinetic Constants ◽  
Extracellular Nucleotide ◽  
Nucleotide Hydrolysis

scholarly journals Degradation of monomeric and fibrillar type III collagens by human skin collagenase. Kinetic constants using different animal substrates.

1985 ◽  
Vol 260 (2) ◽  
pp. 1052-1059
Author(s):  
H G Welgus ◽  
R E Burgeson ◽  
J A Wootton ◽  
R R Minor ◽  
C Fliszar ◽  
...  
Keyword(s):  
Human Skin ◽  
Kinetic Constants ◽  
Type Iii

scholarly journals A New Ultrasensitive Bioluminescence-Based Method for Assaying Monoacylglycerol Lipase

2021 ◽  
Vol 22 (11) ◽  
pp. 6148
Author(s):  
Matteo Miceli ◽  
Silvana Casati ◽  
Pietro Allevi ◽  
Silvia Berra ◽  
Roberta Ottria ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Kinetic Constants ◽  
New Method ◽  
Monoacylglycerol Lipase ◽  
Enzymatic Cleavage ◽  
Highly Sensitive ◽  
Bioluminescence Assay ◽  
Identification And Characterization ◽  
In Cells

A novel bioluminescent Monoacylglycerol lipase (MAGL) substrate 6-O-arachidonoylluciferin, a D-luciferin derivative, was synthesized, physico-chemically characterized, and used as highly sensitive substrate for MAGL in an assay developed for this purpose. We present here a new method based on the enzymatic cleavage of arachidonic acid with luciferin release using human Monoacylglycerol lipase (hMAGL) followed by its reaction with a chimeric luciferase, PLG2, to produce bioluminescence. Enzymatic cleavage of the new substrate by MAGL was demonstrated, and kinetic constants Km and Vmax were determined. 6-O-arachidonoylluciferin has proved to be a highly sensitive substrate for MAGL. The bioluminescence assay (LOD 90 pM, LOQ 300 pM) is much more sensitive and should suffer fewer biological interferences in cells lysate applications than typical fluorometric methods. The assay was validated for the identification and characterization of MAGL modulators using the well-known MAGL inhibitor JZL184. The use of PLG2 displaying distinct bioluminescence color and kinetics may offer a highly desirable opportunity to extend the range of applications to cell-based assays.

scholarly journals Aspartate aminotransferase. The effects of ionic concentration on kinetic constants of both isoenzymes

1968 ◽  
Vol 106 (3) ◽  
pp. 581-586 ◽  
Author(s):  
T. R. C. Boyde
Keyword(s):  
Aspartate Aminotransferase ◽  
Specific Effect ◽  
Ionic Concentration ◽  
Phosphate Concentration ◽  
Kinetic Constants ◽  
Sharp Minimum ◽  
Ionic Concentrations ◽  
Michaelis Constants ◽  
Added Salt

1. The Michaelis constants for both isoenzymes for both substrates depend strongly on ionic concentration, being approximately proportional to phosphate concentration over considerable ranges. This is probably an effect of anions only. 2. In the absence of added salt, Km (2-oxoglutarate) (anionic isoenzyme) is so small as to be indeterminate. 3. Km (l-aspartate) (anionic isoenzyme) passes through a sharp minimum at about 3·3mm-phosphate. It is not clear whether this is a specific effect of phosphate. 4. Both substrates are inhibitory at sufficiently low ionic concentrations. 5. A modified graphical procedure is described for the derivation of the kinetic constants.

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