THE NATURE OF THE MULTIPLE FORMS OF BOVINE THIOL: PROTEIN DISULFIDE OXIDOREDUCTASE

2009 ◽  
Vol 14 (5) ◽  
pp. 409-413 ◽  
Author(s):  
MARIO PACE ◽  
JACK E. DIXON
1980 ◽  
Vol 255 (23) ◽  
pp. 11085-11087
Author(s):  
J. Moss ◽  
S.J. Stanley ◽  
J.E. Morin ◽  
J.E. Dixon

1972 ◽  
Vol 50 (5) ◽  
pp. 507-509 ◽  
Author(s):  
Luis A. Branda ◽  
Barbara M. Ferrier ◽  
Lynne Celhoffer

Thiol–protein disulfide oxidoreductase activity was detected in the soluble cell fraction of human placental tissue homogenized in sucrose. This activity was demonstrated in the rapid reduction of oxytocin and the somewhat less rapid reduction of insulin by reduced glutathione. The apparent pH optimum of the enzymic activity for the reduction of oxytocin and insulin was found to be near pH 8.


1973 ◽  
Vol 51 (11) ◽  
pp. 1555-1558 ◽  
Author(s):  
B. M. Ferrier ◽  
T. Johns ◽  
A. Say ◽  
L. A. Branda

Glutathione–protein disulfide oxidoreductase activity has been demonstrated in mouse mammary gland, with both insulin and oxytocin serving as disulfide-containing substrates. The activity does not change markedly in pregnancy but shows a marked increase when lactation is established, reaching a maximum about the 10th day of lactation.


2006 ◽  
Vol 356 (1) ◽  
pp. 155-164 ◽  
Author(s):  
Emilia Pedone ◽  
Katia D'Ambrosio ◽  
Giuseppina De Simone ◽  
Mosè Rossi ◽  
Carlo Pedone ◽  
...  

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