Instrumental, theoretical, and experimental aspects of determining thermodynamic and kinetic parameters from steady-state and non-steady-state cyclic voltammetry at microelectrodes in high-resistance solvents: application to the fac/mer-[Cr(CO)3(.eta.3-Ph2PCH2CH2P(Ph)CH2CH2PPh2)]+/0 square reaction scheme in dichloromethane

1992 ◽  
Vol 64 (9) ◽  
pp. 1014-1021 ◽  
Author(s):  
Alan M. Bond ◽  
Stephen W. Feldberg ◽  
Howard B. Greenhill ◽  
Peter J. Mahon ◽  
Ray. Colton ◽  
...  



Biochemistry ◽  
2010 ◽  
Vol 49 (49) ◽  
pp. 10421-10439 ◽  
Author(s):  
Jarrod B. French ◽  
Yana Cen ◽  
Tracy L. Vrablik ◽  
Ping Xu ◽  
Eleanor Allen ◽  
...  


1999 ◽  
Vol 274 (25) ◽  
pp. 17711-17717 ◽  
Author(s):  
Timothy J. Pickering ◽  
Scott Garforth ◽  
Jon R. Sayers ◽  
Jane A. Grasby


1984 ◽  
Vol 4 (6) ◽  
pp. 483-488 ◽  
Author(s):  
Nikolaus Kühn-Velten ◽  
Joachim Wolff ◽  
Wolfgang Staib

Kinetic parameters of 3β-hydroxysteroid dehydrogenase/isomerase, steroid-17α-monooxygenase, and steroid-17,20-lyase activities were estimated under steady-state conditions. Purified Leydig cells from rat testes were superfused with pregnenolone, progesterone, or 17α-hydroxyprogesterone. The Km values for both the monooxygenase- and the lyase-catalyzed reactions were by factors of five to ten higher if analyzed with the exogenously added substrate (0.98 and 0.65 μM, respectively) than if calculated from endogenous substrate derived from a precursor (0.10 and 0.13 μM, respectively). This discrepancy may be explained by different substrate partition between the intra- and extraceIJular spaces and by different substrate concentration at the active site of the respective enzyme, depending on whether the actual substrate is of exogenous or endogenous source.



2006 ◽  
Vol 53 (2) ◽  
pp. 407-420 ◽  
Author(s):  
Ramón Varón ◽  
Matilde E Fuentes ◽  
Manuela García-Moreno ◽  
Francisco Garcìa-Sevilla ◽  
Enrique Arias ◽  
...  

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.





1986 ◽  
pp. 293-339
Author(s):  
Satoru Kuhara ◽  
Kiyokazu Nemoto ◽  
Yukihiro Eguchi ◽  
Naoto Sakamoto


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