scholarly journals Mathematical Analysis of Diffusion and Kinetics of Immobilized Enzyme Systems that Follow the Michaelis – Menten Mechanism

2017 ◽  
Vol 6 (3) ◽  
pp. 143 ◽  
Author(s):  
Krishnan Lakshmi Narayanan
Keyword(s):  
Mathematical Analysis ◽  
Immobilized Enzyme ◽  
Enzyme Systems ◽  
Diffusion And Kinetics ◽  
Kinetics Of

Elastic Properties of Steps at Interphase Boundaries

1991 ◽  
Vol 238 ◽  
Author(s):  
G. J. Shiflet
Keyword(s):  
Energy Density ◽  
Elastic Properties ◽  
Mathematical Analysis ◽  
Strain Energy ◽  
Chemical Processes ◽  
Diffusion Kinetics ◽  
Interphase Boundaries ◽  
Kinetics Of ◽  
Maximum Stresses

ABSTRACTStresses are introduced in crystals at interphase boundaries where steps improve the registry of atoms. A model and mathematical analysis based on an approach previously taken by van der Merwe and Shiflet1–4 of the problem incorporating a coherent step are presented. Computed distributions of stresses, strains, dilatation and energy density in the form of contours and nets are given for a coherent monatomic step. It is concluded that the maximum stresses are quite large and the fields decay fairly rapidly with distance from the steps, the gradient of dilatation around steps will significantly affect diffusion kinetics of impurities and the strain energy seems too low to significantly enhance chemical processes.

Stereochemical control of yeast reductions. 2. Quantitative treatment of the kinetics of competing enzyme systems for a single substrate

1984 ◽  
Vol 12 (2) ◽  
pp. 98-117 ◽  
Author(s):  
Ching-Shih Chen ◽  
Bing-nan Zhou ◽  
Gary Girdaukas ◽  
Woan-Ru Shieh ◽  
Frank VanMiddlesworth ◽  
...  
Keyword(s):  
Stereochemical Control ◽  
Enzyme Systems ◽  
Single Substrate ◽  
Kinetics Of ◽  
Quantitative Treatment

Kinetics of enzymatic O-methylation: its value in assays for catecholamines in plasma.

1984 ◽  
Vol 30 (1) ◽  
pp. 24-27 ◽  
Author(s):  
L Mason ◽  
C Weinkove
Keyword(s):  
Mathematical Analysis ◽  
Plasma Catecholamines ◽  
High Concentration ◽  
Internal Standards ◽  
Linear Approximations ◽  
Endogenous Catecholamine ◽  
Radioenzymatic Assay ◽  
Exponential Equations ◽  
Kinetics Of ◽  
Catecholamine Concentration

Abstract The kinetics of enzymatic O-methylation of catecholamines were studied under conditions like those used in the radioenzymatic assay of plasma catecholamines. Inappropriate Michaelis-Menten kinetics and linear approximations of exponential equations were not used. Mathematical analysis indicated the importance of the ratio of methyl donor (S-adenosylmethionine) to substrate (catecholamine) concentration. If the reaction is incomplete, only a large ratio will allow linear approximations between product formed and initial catecholamine concentration. The use of high-concentration internal standards to correct for plasma interference may give erroneous results by reducing this ratio. Accuracy will be improved by ensuring (a) that S-adenosylmethionine is always greatly in excess of catecholamine, (b) that concentrations of added standards are of the same order as for endogenous catecholamine, and (c) that a high activity of enzyme is used, to allow the reaction to reach completion even in the presence of some inhibition.

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