A kinetic study on the action of rubber oxidation inhibitors—III. Kinetics of inhibited oxidation

The kinetics of the unimolecular isomerization reaction[Formula: see text]have been studied. The ΔH≠ values in kcal mol−1 are 36.8 ± 2.0 (M = M′ = Mn ), 46.8 ± 0.5 (M = M′ = Re ), 39.2 ± 2.8 (M = Mn, M′ = Re ). The mechanism of the rearrangement is discussed.

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Kinetic Study of the Diels-Alder Reaction of Cyclopentadiene with Bis(2-Ethylhexyl) Maleate

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.634-638.541 ◽

2013 ◽

Vol 634-638 ◽

pp. 541-545 ◽

Cited By ~ 3

Author(s):

Jun Seong Park ◽

Dae Hee Yun ◽

Tae Won Ko ◽

Yong Sung Park ◽

Je Wan Woo

Keyword(s):

Kinetic Study ◽

Reaction Temperature ◽

Atmospheric Pressure ◽

Arrhenius Equation ◽

Alder Reaction ◽

Diels Alder ◽

Influence Of Temperature ◽

Diels Alder Reaction ◽

Influence Of Temperature On ◽

Kinetics Of

The kinetics of the Diels-Alder reaction of cyclopentadiene with bis(2-ethylhexyl) maleate has been studied at temperatures between 25 and 100 °C and at atmospheric pressure. The influence of temperature on the kinetic constants was determined by fitting the results to the Arrhenius equation. As a result, fitting line similar with the linear curve of the Arrhenius equation at 25, 30 and 40 °C. However, the fitting curve, at 60, 80 and 100 °C, tended towards the outside of the curve in the form of Arrhenius equation. The ratio of endo/exo was a slight change from increase of the reaction temperature.

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Liquid-phase thermogravimetric measurement of reaction kinetics of the conversion of biomass wastes in pressurized hot water: a kinetic study

Advances in Environmental Research ◽

10.1016/s1093-0191(02)00014-x ◽

2003 ◽

Vol 7 (2) ◽

pp. 421-428 ◽

Cited By ~ 29

Author(s):

Kazuhiro Mochidzuki ◽

Akiyoshi Sakoda ◽

Motoyuki Suzuki

Keyword(s):

Liquid Phase ◽

Kinetic Study ◽

Reaction Kinetics ◽

Hot Water ◽

Kinetics Of

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Kinetic Study of Application of ZnO as a Photocatalyst in Heterogeneous Medium

E-Journal of Chemistry ◽

10.1155/2009/139753 ◽

2009 ◽

Vol 6 (2) ◽

pp. 531-536 ◽

Cited By ~ 20

Author(s):

J. J. Vora ◽

S. K. Chauhan ◽

K. C. Parmar ◽

S. B. Vasava ◽

S. Sharma ◽

...

Keyword(s):

Light Intensity ◽

Photocatalytic Degradation ◽

Kinetic Study ◽

Heterogeneous Medium ◽

Degradation Process ◽

Probable Mechanism ◽

Band Gaps ◽

Light Control ◽

Substrate Ph ◽

Kinetics Of

The photocatalytic degradation of 2,4-dinitrophenol over ZnO was carried out in the presence of light. Control experiments were carried out. The photocatalytic degradation of 2,4-dinitrophenol was observed spectro-photmerically. The various parameters like concentrations of substrate, pH, amounts and band gaps of semiconductor, impact of light intensity, sensitizers and radical quenchers affected the kinetics of the degradation process. A probable mechanism for this process has been proposed.

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Kinetics of a self-amplifying substrate cycle: ADP–ATP cycling assay

Biochemical Journal ◽

10.1042/bj3500237 ◽

2000 ◽

Vol 350 (1) ◽

pp. 237-243 ◽

Cited By ~ 1

Author(s):

Edelmira VALERO ◽

Ramón VARÓN ◽

Francisco GARCÍA-CARMONA

Keyword(s):

Lactate Dehydrogenase ◽

Kinetic Study ◽

Pyruvate Kinase ◽

Adenylate Kinase ◽

Reaction Medium ◽

Spectrophotometric Assay ◽

Background Signal ◽

Cyclic System ◽

Exponential Increase ◽

Kinetics Of

A kinetic study of an ATP–ADP amplification cyclic system involving the enzymes adenylate kinase, pyruvate kinase and l-lactate dehydrogenase has been made. The stoichiometry of the cycle is 2:1, because two molecules of ADP are synthesized from one each of ATP and AMP, and one molecule of ADP is converted back into one of ATP at each turn of the cycle. This results in a continuous exponential increase in the concentrations of ATP and ADP in the reaction medium, according to the equations obtained. This is therefore a substrate cycle that amplifies itself, the cycling rate increasing continuously with time. The background signal of the reagent was reduced by using apyrase to degrade ATP and ADP in the reagent, permitting detection limits as low as 16pmol of ATP and/or ADP in a continuous spectrophotometric assay.

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A kinetic study of rabbit muscle pyruvate kinase

Biochemical Journal ◽

10.1042/bj1310223 ◽

1973 ◽

Vol 131 (2) ◽

pp. 223-236 ◽

Cited By ~ 48

Author(s):

S. Ainsworth ◽

N. Macfarlane

Keyword(s):

Reaction Mechanism ◽

Kinetic Study ◽

Pyruvate Kinase ◽

Random Order ◽

Experimental Results ◽

Rabbit Muscle ◽

Dead End ◽

Inhibition Constants ◽

Muscle Pyruvate Kinase ◽

Kinetics Of

The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by rabbit muscle pyruvate kinase. The experimental results indicate that the reaction mechanism is equilibrium random-order in type, that the substrates and products are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg2+, form randomly and exist in equilibrium with themselves and other substrate complexes. Values were determined for the Michaelis, dissociation and inhibition constants of the reaction and are compared with values ascertained by previous workers.

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