The determination of kinetic constants governing the slow,tight-binding inhibition of enzyme-catalysed reactions

Author(s):  
Michael J. Sculley ◽  
John F. Morrison
2021 ◽  
Vol 139 ◽  
pp. 111664
Author(s):  
Haiyang Yang ◽  
Xueyan Li ◽  
Gang Li ◽  
Huating Huang ◽  
Wenning Yang ◽  
...  

2000 ◽  
Vol 281 (1) ◽  
pp. 62-67 ◽  
Author(s):  
Petr Kuzmič ◽  
Steve Sideris ◽  
Lynne M. Cregar ◽  
Kyle C. Elrod ◽  
Kenneth D. Rice ◽  
...  

2017 ◽  
Vol 16 (1) ◽  
pp. 121-130 ◽  
Author(s):  
Seyyed Mohammad Mousavi ◽  
Seyed Omid Rastegar ◽  
Seyed Abbas Shojaosadati ◽  
Soheila Sheibani

1986 ◽  
Vol 261 (33) ◽  
pp. 15505-15507
Author(s):  
L L Slakey ◽  
K Cosimini ◽  
J P Earls ◽  
C Thomas ◽  
E L Gordon

1988 ◽  
Vol 253 (2) ◽  
pp. 517-522 ◽  
Author(s):  
J M Fominaya ◽  
J M García-Segura ◽  
M Ferreras ◽  
J G Gavilanes

A general treatment of very tight-binding inhibition is described. It was applied to purified endogenous RNAase inhibitor from rat testis. This treatment discriminates among the different types of inhibition and allows for calculation of the inhibition parameters. When very tight-binding inhibitions are studied at similar molar concentrations of both enzyme and inhibitor, a further approach is required. This is also described and applied to the RNAase inhibitor. A Ki value of 3.2 x 10(-12) M was found for this inhibitor protein. On the basis of this result, it was considered inappropriate to classify this type of inhibitor in terms of competitive or non-competitive, as has been done for such inhibitors so far. Functional consequences of this analysis are discussed for the RNAase-RNAase inhibitor system.


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