Hexokinase activity alters sugar-nucleotide formation in maize root homogenates

2000 ◽  
Vol 53 (1) ◽  
pp. 29-37 ◽  
Author(s):  
Antonio Galina ◽  
Wagner Seixas da Silva
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.


1950 ◽  
Author(s):  
Gabriel Baldovinos de la Pena
Keyword(s):  

1995 ◽  
Vol 108 (1) ◽  
pp. 241-246 ◽  
Author(s):  
A. R. Facanha ◽  
L. de Meis
Keyword(s):  

Author(s):  
Junnosuke Otaka ◽  
Guntur Venkata Subbarao ◽  
Hiroshi Ono ◽  
Tadashi Yoshihashi

AbstractTo control agronomic N losses and reduce environmental pollution, biological nitrification inhibition (BNI) is a promising strategy. BNI is an ecological phenomenon by which certain plants release bioactive compounds that can suppress nitrifying soil microbes. Herein, we report on two hydrophobic BNI compounds released from maize root exudation (1 and 2), together with two BNI compounds inside maize roots (3 and 4). On the basis of a bioassay-guided fractionation method using a recombinant nitrifying bacterium Nitrosomonas europaea, 2,7-dimethoxy-1,4-naphthoquinone (1, ED50 = 2 μM) was identified for the first time from dichloromethane (DCM) wash concentrate of maize root surface and named “zeanone.” The benzoxazinoid 2-hydroxy-4,7-dimethoxy-2H-1,4-benzoxazin-3(4H)-one (HDMBOA, 2, ED50 = 13 μM) was isolated from DCM extract of maize roots, and two analogs of compound 2, 2-hydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (HMBOA, 3, ED50 = 91 μM) and HDMBOA-β-glucoside (4, ED50 = 94 μM), were isolated from methanol extract of maize roots. Their chemical structures (1–4) were determined by extensive spectroscopic methods. The contributions of these four isolated BNI compounds (1–4) to the hydrophobic BNI activity in maize roots were 19%, 20%, 2%, and 4%, respectively. A possible biosynthetic pathway for zeanone (1) is proposed. These results provide insights into the strength of hydrophobic BNI activity released from maize root systems, the chemical identities of the isolated BNIs, and their relative contribution to the BNI activity from maize root systems.


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.


2000 ◽  
Vol 123 (3) ◽  
pp. 1037-1046 ◽  
Author(s):  
Yayoi Onda ◽  
Tomohiro Matsumura ◽  
Yoko Kimata-Ariga ◽  
Hitoshi Sakakibara ◽  
Tatsuo Sugiyama ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document