scholarly journals Function of the phosphate group of pyridoxal 5'-phosphate in the glycogen phosphorylase reaction.

1981 ◽  
Vol 256 (2) ◽  
pp. 728-730
Author(s):  
M. Takagi ◽  
S. Shimomura ◽  
T. Fukui
Author(s):  
Kuixiong Gao ◽  
Randal E. Morris ◽  
Bruce F. Giffin ◽  
Robert R. Cardell

Several enzymes are involved in the regulation of anabolic and catabolic pathways of carbohydrate metabolism in liver parenchymal cells. The lobular distribution of glycogen synthase (GS), phosphoenolpyruvate carboxykinase (PEPCK) and glycogen phosphorylase (GP) was studied by immunocytochemistry using cryosections of normal fed and fasted rat liver. Since sections of tissue embedded in polyethylene glycol (PEG) show good morphological preservation and increased detectability for immunocytochemical localization of antigenic sites, and semithin sections of Visio-Bond (VB) embedded tissue provide higher resolution of cellular structure, we applied these techniques and immunogold-silver stain (IGSS) for a more accurate localization of hepatic carbohydrate metabolic enzymes.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
SE Zographos ◽  
DD Leonidas ◽  
KM Alexacou ◽  
T Gimisis ◽  
JM Hayes ◽  
...  

2017 ◽  
Vol 24 (4) ◽  
pp. 384-403 ◽  
Author(s):  
Demetres Leonidas ◽  
Joseph Hayes ◽  
Atsushi Kato ◽  
Vassiliki Skamnaki ◽  
Demetra Chatzileontiadou ◽  
...  

1979 ◽  
Vol 44 (2) ◽  
pp. 613-625 ◽  
Author(s):  
Valentina I. Gulyaeva ◽  
Antonín Holý

The present paper studies the effect of the modification of heterocyclic base, sugar moiety and the presence of phosphate group on the nucleoside acceptors in the synthesis of dinucleoside phosphates from adenosine 2',3'-cyclic phosphate as donor, catalyzed by nonspecific acidic extracellular and intracellular ribonucleases from Penicillium claviforme. The enzyme binds specifically the acceptor molecule, preferring cytosine nucleosides. It requires the presence of the whole sugar moiety, an exact mutual orientation of the heterocyclic base and the reaction center (5'-hydroxy group), and a suitable conformation of the acceptor molecule. The enzyme-acceptor bond is homochiral and the presence of the N3-H group in the pyrimidine ring is important. The reaction between the donor and the acceptor is bimolecular and is competitively inhibited by some purine nucleosides.


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