Cytoimmunochemical study of pyruvate kinase isoenzymes in rat liver

2008 ◽  
Vol 2 (4) ◽  
pp. 340-345 ◽  
Author(s):  
P. Gali ◽  
L. Hartmann
1986 ◽  
Vol 7 (8) ◽  
pp. 1351-1357 ◽  
Author(s):  
M. Reinacher ◽  
E. Eigenbrodt ◽  
U. Gerbracht ◽  
G. Zenk ◽  
I. Timmermann-Trosiener ◽  
...  

1980 ◽  
Vol 190 (1) ◽  
pp. 125-130 ◽  
Author(s):  
B Mannervik ◽  
K Axelsson

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978–2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding indicates a role of the thioltransferase in the regulation of the ‘glutathione status’ of the cell. Specifically, it was found that thioltransferase catalyses the reactivation of pyruvate kinase from rat liver that had previously been inactivated by glutathione disulphide. It is suggested that thioltransferase may have a general role in regulatory processes involving thiol-disulphide interchange.


Biochemistry ◽  
1975 ◽  
Vol 14 (18) ◽  
pp. 4041-4045 ◽  
Author(s):  
Janet M. Cardenas ◽  
J. Jeffrey Strandholm ◽  
Joan M. Miller

Sign in / Sign up

Export Citation Format

Share Document