Dopamine D1 receptors labelled with [3H]SCH23390 in rabbit cerebral cortex and neostriatum Equilibrium binding, kinetics and selectivity

1989 ◽  
Vol 340 (6) ◽  
pp. 617-625 ◽  
Author(s):  
Tom�s A. Reader ◽  
Louise Grondin ◽  
Bernard Montreuil ◽  
Karen M. Dewar
2020 ◽  
Vol 156 ◽  
pp. 58-65 ◽  
Author(s):  
Nae Saito ◽  
Kazuki Tainaka ◽  
Tom Macpherson ◽  
Takatoshi Hikida ◽  
Shun Yamaguchi ◽  
...  

1997 ◽  
Vol 2 (4) ◽  
pp. 291-292 ◽  
Author(s):  
Y Okuba ◽  
T Suhara ◽  
Y Sudo ◽  
M Toru

1992 ◽  
Vol 283 (2) ◽  
pp. 561-566 ◽  
Author(s):  
A Sosa ◽  
H Ordaz ◽  
I Romero ◽  
H Celis

The substrate for the hydrolytic activity of membrane-bound pyrophosphatase is the PP(i)-Mg2+ complex. The enzyme has no activity when the free Mg2+ concentration is lower than 10 microM (at 0.5 mM-PP(i)-Mg2+), and therefore free Mg2+ is an essential activator of the hydrolytic activity. The Km for the substrate changes in response to variation in free Mg2+ concentration, from 10.25 to 0.6 mM when free Mg2+ is increased from 0.03 to 1.0 mM respectively. The Km for Mg2+ depends on the substrate concentration: the Km decreases from 0.52 to 0.14 mM from 0.25 to 0.75 mM-PP(i)-Mg2+ respectively. The extrapolated Km for Mg2+ in the absence of the substrate is 0.73 mM. Imidodiphosphate-Mg2+ and free Ca2+ were used as competitive inhibitors of substrate and activator respectively. The equilibrium binding kinetics suggest an ordered mechanism for the activator and the substrate: Mg2+ ions bind the enzyme before PP(i)-Mg2+ in the formation of the catalytic complex, membrane-bound pyrophosphatase-(Mg2+)-(PP(i)-Mg2+).


1993 ◽  
Vol 242 (2) ◽  
pp. 165-172 ◽  
Author(s):  
Val J. Watts ◽  
Cindy P. Lawler ◽  
John H. Gilmore ◽  
Stan B. Southerland ◽  
David E. Nichols ◽  
...  

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