A kinetic study of an unstable enzyme measured through coupling reactions. Application to the self-inactivation of detergent-solubilized Ca2+-ATPase from sarcoplasmic reticulum

Author(s):  
Senena Corbalán-García ◽  
JoséA. Teruel ◽  
Ramón Varón ◽  
Francisco García-Cánovas ◽  
Juan C. Gómez-Fernández
2018 ◽  
Vol 122 (23) ◽  
pp. 5089-5097 ◽  
Author(s):  
Chuying Dai ◽  
Yajiao Hao ◽  
Yang Yu ◽  
Minjie Li ◽  
Sean Xiao-An Zhang

2003 ◽  
Vol 107 (14) ◽  
pp. 2470-2477 ◽  
Author(s):  
Eric Villenave ◽  
Sandy Moisan ◽  
Robert Lesclaux
Keyword(s):  

2010 ◽  
Vol 958 (1-3) ◽  
pp. 106-115 ◽  
Author(s):  
Abdallah Alsoufi ◽  
Mohammednoor Altarawneh ◽  
Bogdan Z. Dlugogorski ◽  
Eric M. Kennedy ◽  
John C. Mackie

Catalysts ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 435
Author(s):  
Marc Renom Carrasco ◽  
Clémence Nikitine ◽  
Mohamed Hamou ◽  
Claude de Bellefon ◽  
Chloé Thieuleux ◽  
...  

A kinetic study concerning the self-metathesis of methyl oleate and methyl elaidate was performed, using a variety of NHC-ruthenium pre-catalysts, bearing either mesityl groups or di-isopropyl-phenyl groups on the NHC ligand and various trans ligands with respect to the NHC unit. We showed that the system can be satisfactorily described using one initiation constant per pre-catalyst and four propagation constants that, conversely, do not depend on the pre-catalyst. The difference of reactivity with oleate (Z) and elaidate (E) can be fully explained by the propagation parameters; the studied pre-catalysts initiate with the same rate starting from the Z or the E olefin. The ranking of the propagation parameters is driven by the thermodynamic equilibrium. The transformation rates of Z and E isomers is only driven by these propagation constants and nothing differentiates the initiation step.


1987 ◽  
Vol 15 (3) ◽  
Author(s):  
C. Berthet-Colominas ◽  
M. Cuillel ◽  
M.H.J. Koch ◽  
P. Vachette ◽  
B. Jacrot

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