Effect of hexokinase activity on tomato root metabolism during prolonged hypoxia

2007 ◽  
Vol 30 (4) ◽  
pp. 508-517 ◽  
Author(s):  
IMENE GHARBI ◽  
BERENICE RICARD ◽  
DOMINIQUE ROLIN ◽  
MICHAEL MAUCOURT ◽  
MARIE-HELENE ANDRIEU ◽  
...  
Author(s):  
Krishan K. Arora ◽  
Glenn L. Decker ◽  
Peter L. Pedersen

Hexokinase (ATP: D-hexose 6-phophotransferase EC 2.7.1.1) is the first enzyme of the glycolytic pathway which commits glucose to catabolism by catalyzing the phosphorylation of glucose with ATP. Previous studies have shown diat hexokinase activity is markedly elevated in rapidly growing tumor cells exhibiting high glucose catabolic rates. A large fraction (50-80%) of this enzyme activity is bound to the mitochondrial fraction (1,2) where it has preferred access to ATP (3). In contrast,the hexokinase activity of normal tissues is quite low, with one exception being brain which is a glucose-utilizing tissue (4). Biochemical evidence involving rigorous subfractionation studies have revealed striking differences between the subcellular distribution of hexokinase in normal and tumor cells [See review by Arora et al (4)].In the present report, we have utilized immunogold labeling techniques to evaluate die subcellular localization of hexokinase in highly glycolytic AS-30D hepatoma cells and in the tissue of its origin, i.e., rat liver.


1952 ◽  
Vol 30 (6) ◽  
pp. 561-570
Author(s):  
J. G. Aldous ◽  
D. K. R. Stewart

Suspensions of the cells of baker’s yeast were irradiated with ultraviolet light for sufficient times to produce populations of 75, 50, 30, and 5% viable cells. After washing and drying, various enzyme solutions were prepared from these cells. Enzymatic activities, on a nitrogen basis, were compared to those of solutions prepared from a nonirradiated population. At the 50% survival level, hexokinase, carboxylase, and zymase were inhibited to a degree roughly proportional to the viability. Carboxylase, and to a certain extent, hexokinase activity varied directly as the population viability. Catalase, alcohol dehydrogenase, and lactic dehydrogenase showed no diminution in activity even at the 5% survival level. These results suggest that although ultraviolet radiation may produce nuclear damage, the primary site of action may be certain enzymes of the cytoplasm.


The Analyst ◽  
2014 ◽  
Vol 139 (21) ◽  
pp. 5582-5586 ◽  
Author(s):  
Sai Lian ◽  
Wenxia Yang ◽  
Yucong Wang ◽  
Chenghui Liu ◽  
Zhengping Li

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