Studies on the Interactions between Phospholipids and Membrane-Bound Enzymes in Microsomes. Effects of Phospholipases C on Kinetic Properties of the Glucose-6-Phosphatase System in Rat Liver Microsomes1

1983 ◽  
Vol 93 (2) ◽  
pp. 537-546 ◽  
Author(s):  
Kohei SAWAKI ◽  
Ryo TAGUCHI ◽  
Hiroh IKEZAWA
1985 ◽  
Vol 34 (15) ◽  
pp. 2685-2689 ◽  
Author(s):  
Jorge L. Gonzalez-Calvin ◽  
John B. Saunders ◽  
Ian R. Crossley ◽  
Christopher J. Dickenson ◽  
Heather M. Smith ◽  
...  

FEBS Letters ◽  
1976 ◽  
Vol 72 (2) ◽  
pp. 262-266 ◽  
Author(s):  
F. Feo ◽  
R.A. Canuto ◽  
R. Garcea ◽  
A. Avogadro ◽  
M. Villa ◽  
...  

1980 ◽  
Vol 12 (8) ◽  
pp. 739-749 ◽  
Author(s):  
Lanfranco Corazzi ◽  
Giuseppe Arienti ◽  
Giuseppe Porcellati

1978 ◽  
Vol 27 (5) ◽  
pp. 641-645 ◽  
Author(s):  
Georges Guellaen ◽  
Jean-Louis Mahu ◽  
Philippe Mavier ◽  
Jacques Hanoune ◽  
Pierre Berthelot

2009 ◽  
Vol 37 (3) ◽  
pp. 222-232 ◽  
Author(s):  
Jukka Marniemi ◽  
Antero Aitio ◽  
Harri Vainio

1983 ◽  
Vol 214 (2) ◽  
pp. 649-652 ◽  
Author(s):  
J D McGivan ◽  
N M Bradford

Liver glutaminase can be solubilized from frozen-and-thawed mitochondria by treatment with phospholipase A2. Solubilization by this technique markedly changes the kinetic properties of the enzyme. The properties of the membrane-bound form of the enzyme are partially restored by adding phosphatidylcholine or phosphatidylethanolamine to the phospholipase extract. It is concluded that the kinetic properties of liver glutaminase are a function of the interaction of this enzyme with membrane phospholipids.


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