Kinetics of magnesium(2+) ion flux into rat liver mitochondria

Biochemistry ◽  
1979 ◽  
Vol 18 (12) ◽  
pp. 2590-2595 ◽  
Author(s):  
Joyce Johnson Diwan ◽  
Michel Daze ◽  
Ronald Richardson ◽  
David Aronson
1973 ◽  
Vol 134 (4) ◽  
pp. 1023-1029 ◽  
Author(s):  
Norah M. Bradford ◽  
J. D. McGivan

1. The kinetics of glutamate transport into mitochondria were determined by using Bromocresol Purple to terminate the transport process. 2. Glutamate transport was found to have a Vmax. of 9.1nmol/min per mg of protein at pH6.9 and 20°C; the Km for glutamate was 4mm. 3. The rate of glutamate deamination in intact mitochondria was tenfold slower than in disrupted mitochondria. 4. These results suggest that glutamate deamination may be controlled by the rate of glutamate transport. Possible consequences of these findings are discussed.


Biochemistry ◽  
1979 ◽  
Vol 18 (26) ◽  
pp. 5972-5978 ◽  
Author(s):  
Marco Bragadin ◽  
Tullio Pozzan ◽  
Giovanni Felice Azzone

1970 ◽  
Vol 48 (6) ◽  
pp. 659-663 ◽  
Author(s):  
L. Sierens ◽  
A. D'Iorio

Indirect evidence from the kinetics of oxidative deamination is presented for the existence of two different monoamine oxidases in rat liver mitochondria. The enzymes can be differentiated on the basis of their affinities for benzylamine and serotonin. Electrophoretic separation yielded two fractions, each with the characteristics predicted from the kinetic experiments.


FEBS Letters ◽  
1971 ◽  
Vol 13 (2) ◽  
pp. 92-94 ◽  
Author(s):  
H. Bugany ◽  
L. Flohe ◽  
U. Weser

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