γ-GLUTAMYL PEPTIDES AND RELATED AMINO ACIDS IN RAT HIPPOCAMPUS IN VITRO: EFFECT OF DEPOLARIZATION AND γ-GLUTAMYL TRANSPEPTIDASE INHIBITION

1996 ◽  
Vol 29 (2) ◽  
pp. 121-128 ◽  
Author(s):  
XIAOYING LI ◽  
OWE ORWAR ◽  
CAMILLA REVESJÖ ◽  
MATS SANDBERG
Neuropeptides ◽  
1998 ◽  
Vol 32 (5) ◽  
pp. 431-434 ◽  
Author(s):  
C.H Hadjiivanova ◽  
V Georgiev

1995 ◽  
Vol 674 (1) ◽  
pp. 104-106 ◽  
Author(s):  
César Sepúlveda ◽  
Gonzalo Bustos ◽  
Katia Gysling ◽  
Mario Seguel ◽  
Rodrigo Labarca

1981 ◽  
Vol 198 (1) ◽  
pp. 243-246 ◽  
Author(s):  
C R Baumrucker ◽  
P A Pocius ◽  
T L Riss

gamma-Glutamyltransferase (D-glutamyl transpeptidase, EC 2.3.2.2) activity has been shown to be located predominantly on the extracellular surface of the plasma membrane of lactating bovine mammary cells. Radioactive label from both oxidized ([14C]-gamma-glutamyl) and reduced ([35S]cysteinyl) glutathione was taken up and incorporated into acid-precipitable proteins of mammary tissue. Uptake was shown to involve the transport of free amino acids, and incorporation was shown to involve the action of gamma-=glutamyltransferase. These results indicate that lactating mammary tissue utilizes the constituent amino acids of glutathione for milk-protein synthesis.


Sign in / Sign up

Export Citation Format

Share Document