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Wyszukujesz frazę "enzyme activation" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters.
Autorzy:
Fontes, Rui
Ribeiro, João
Sillero, Antonio
Powiązania:
https://bibliotekanauki.pl/articles/1044438.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
enzyme inhibition
enzyme modifier
rapid equilibrium kinetics
I50
enzyme activation
enzyme kinetics
graphical presentations
Opis:
A combined analysis of enzyme inhibition and activation is presented, based on a rapid equilibrium model assumption in which one molecule of enzyme binds one molecule of substrate (S) and/or one molecule of a modifier X. The modifier acts as activator (essential or non-essential), as inhibitor (total or partial), or has no effect on the reaction rate (v), depending on the values of the equilibrium constants, the rate constants of the limiting velocity steps, and the concentration of substrate ([S]). Different possibilities have been analyzed from an equation written to emphasize that v = Ł([X]) is, in general and at a fixed [S], a hyperbolic function. Formulas for Su (the value of [S], different from zero, at which v is unaffected by the modifier) and vsu (v at that particular [S]) were deduced. In Lineweaver-Burk plots, the straight lines related to different [X] generally cross in a point (P) with coordinates (Su, vsu). In certain cases, point P is located in the first quadrant which implies that X acts as activator, as inhibitor, or has no effect, depending on [S]. Furthermore, we discuss: (1) the apparent Vmax and Km displayed by the enzyme in different situations; (2) the degree of effect (inhibition or activation) observed at different concentrations of substrate and modifier; (3) the concept of Ke, a parameter that depends on the concentration of substrate and helps to evaluate the effect of the modifier: it equals the value of [X] at which the increase or decrease in the reaction rate is half of that achieved at saturating [X]. Equations were deduced for the general case and for particular situations, and used to obtain computer-drawn graphs that are presented and discussed. Formulas for apparent Vmax, Km and Ke have been written in a way making it evident that these parameters can be expressed as pondered means.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 233-257
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Contribution of the intra- and intermolecular routes in autocatalytic zymogen activation: application to pepsinogen activation
Autorzy:
Varón, Ramón
Fuentes, Matilde
García-Moreno, Manuela
Garcìa-Sevilla, Francisco
Arias, Enrique
Valero, Edelmira
Arribas, Enrique
Powiązania:
https://bibliotekanauki.pl/articles/1041258.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
intermolecular activation
intramolecular activation
autocatalysis
enzyme kinetics
proenzyme activation
Opis:
Taking as the starting point a recently suggested reaction scheme for zymogen activation involving intra- and intermolecular routes and the enzyme-zymogen complex, we carry out a complete analysis of the relative contribution of both routes in the process. This analysis suggests the definition of new dimensionless parameters allowing the elaboration, from the values of the rate constants and initial conditions, of the time course of the contribution of the two routes. The procedure mentioned above related to a concrete reaction scheme is extrapolated to any other model of autocatalytic zymogen activation involving intra- and intermolecular routes. Finally, we discuss the contribution of both of the activating routes in pepsinogen activation into pepsin using the values of the kinetic parameters given in the literature.
Źródło:
Acta Biochimica Polonica; 2006, 53, 2; 407-420
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Wyznaczanie parametrów termicznej dezaktywacji enzymów
Determination of thermal deactivation parameters of enzymes
Autorzy:
Miłek, J.
Wójcik, M.
Powiązania:
https://bibliotekanauki.pl/articles/2070468.pdf
Data publikacji:
2009
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
dezaktywacja enzymów
parametry kinetyczne
energia aktywacji
enzyme deactivation
kinetic parameters
activation energy
Opis:
Poznanie wpływu temperatury na aktywność enzymu jest bardzo ważne przy optymalnym projektowaniu bioreaktora. W pracy przedstawiono nową metodę wyznaczania parametrów termicznej dezaktywacji enzymów. Algorytm zastosowano do obliczenia energii aktywacji oraz optymalnej temperatury na podstawie użytych danych doświadczalnych wyznaczonych dla oksydazy fenolowej.
Knowledge of the effect of temperature on enzyme activity is very important for optimal design of a bioreactor. In this work, a novel method is proposed to determine parameters of thermal deactivation of enzymes. The algorithm applied for the calculation of activation energies and optimal temperature was verified with the use of experimental data for phenol oxidase.
Źródło:
Inżynieria i Aparatura Chemiczna; 2009, 3; 69-70
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Application of Daftardar-Gejiji and Jafari method to kinetic analysis of thermal inactivation of Jack bean urease
Autorzy:
Sobamowo, G.
Adeleye, O.
Powiązania:
https://bibliotekanauki.pl/articles/973622.pdf
Data publikacji:
2018
Wydawca:
Politechnika Częstochowska. Wydawnictwo Politechniki Częstochowskiej
Tematy:
kinetics
thermal activation
Jack bean urease
enzyme
biotechnology
Daftardar-Gejiji and Jafari method
Kinetyka
analiza kinetyczna
inaktywacja termiczna
enzym
ureaza
biotechnologia
metoda Daftardar-Gejiji i Jafari
Opis:
Jack bean urease has been used as a good catalyst for hydrolysis of urea in various applications such as biotechnology and biomedical engineering. The wide range of applications require proper understanding of the thermal inactivation of the enzyme. Consequently, the theoretical analysis of the enzyme kinetic of the thermal inactivation is required. In this paper, a new iterative method proposed by Daftardar-Gejiji and the Jafari method is applied to analyse the kinetic of thermal inactivation of jack bean urease (EC3.5.1.5). The kinetics of the urease consist of three-reaction steps and included the Arrhenius equation for temperature-dependent rate constants as well as the temperature change in the initial heating period. The approximate analytical solutions are verified with results of numerical method using Runge-Kutta with the shooting method, and good agreements are established between the results of the methods. From the analytical investigation, it is established that the molar concentration of the native enzyme decreases as the time increases while the molar concentration of the denatured enzyme increases as the time increases. The time taken to reach the maximum value of the molar concentration of the native enzyme is the same as the time taken to reach the minimum value of the molar concentration of the denature enzyme. It is hoped that the information given in this theoretical investigation will assist in the kinetic analysis of thermal inactivation of the experimental results over handling rate constants and molar concentrations.
Źródło:
Journal of Applied Mathematics and Computational Mechanics; 2018, 17, 2; 65-76
2299-9965
Pojawia się w:
Journal of Applied Mathematics and Computational Mechanics
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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