scholarly journals Effects of Chloramine-T And CuSO4 On Enzyme Activity Of Glucose 6-Phosphate Dehydrogenase From Rainbow Trout (Oncorhynchus Myskiss) Erythrocytes In Vitro An In Vivo

2003 ◽  
Author(s):  
Mehmet Çiftçi ◽  
Olcay Hisar ◽  
Orhan Erdogan ◽  
Abdulkadir Çiltas
Keyword(s):  
Enzyme Activity ◽  
Rainbow Trout ◽  
Chloramine T ◽  
Glucose 6 Phosphate Dehydrogenase

Paradoxical effect of perchlorate on thyroidal weight, glucose 6-phosphate dehydrogenase and polyamines in methylthiouracil-treated rats

1981 ◽  
Vol 97 (4) ◽  
pp. 491-495 ◽  
Author(s):  
S. Matsuzaki ◽  
M. Suzuki
Keyword(s):  
Enzyme Activity ◽  
Control Level ◽  
Sodium Perchlorate ◽  
Inhibitory Effect ◽  
Paradoxical Effect ◽  
G6pdh Activity ◽  
Wet Weight ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract. The effect of sodium perchlorate (NaClO4) on the methylthiouracil-induced increase in the activity of thyroid glucose 6-phosphate dehydrogenase (G6PDH), ornithine decarboxylase (ODC) and polyamine contents was studied in the rat. The G6PDH activity was increased nearly three-fold by methylthiouracil (MTU) but not by ClO4- at 7 days of treatment. Perchlorate lowered the MTU-induced enzyme activity to nearly the control level, without changing circulating thyrotrophin (TSH). The anion had no inhibitory effect on G6PDH activity in vitro. The possibility that an inhibitor specific for G6PDH was generated in ClO4- treated rat thyroids was excluded. The activity of ODC was greatly increased by both ClO4- and MTU, the increase being significant as early as on the second day of treatment. Perchlorate had no inhibitory effect on MTU-induced ODC activity in vivo but decreased total contents of spermidine and spermine in the thyroid, without affecting the concentration (nmoles/ g wet weight) of the polyamines. These results suggest that ClO4- acts directly on the thyroid to suppress specifically the stimulatory effect of TSH on G6PDH activity and possibly on polyamine accumulation.

Effects of metamizol and magnesium sulfate on enzyme activity of glucose 6-phosphate dehydrogenase from human erythrocyte in vitro and rat erythrocyte in vivo

2001 ◽  
Vol 34 (4) ◽  
pp. 297-302 ◽  
Author(s):  
Mehmet Çiftçi ◽  
İsmail Özmen ◽  
M.Emin Büyükokuroğlu ◽  
Sadrettin Pençe ◽  
Ö.İrfan Küfrevioğlu
Keyword(s):  
Enzyme Activity ◽  
Magnesium Sulfate ◽  
Human Erythrocyte ◽  
Glucose 6 Phosphate Dehydrogenase

Effect of vitamin E on carbonic anhydrase enzyme activity in rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo

2004 ◽  
Vol 52 (4) ◽  
pp. 413-422 ◽  
Author(s):  
Ş. Aras-Hisar ◽  
O. Hisar ◽  
Ş. Beydemir ◽  
I. Gülçin ◽  
T. Yanik
Keyword(s):  
Enzyme Activity ◽  
Rainbow Trout ◽  
Vitamin E ◽  
Carbonic Anhydrase ◽  
Oncorhynchus Mykiss ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Blood Erythrocyte ◽  
The Difference

Considering that the excessive usage of vitamin E causes hypervitaminosis and thus reduces blood erythrocyte concentrations, therefore it is worth studying how its pharmacological dosage affects the activity of carbonic anhydrase (CA) enzyme found in erythrocytes of rainbow trout (Oncorhynchus mykiss) in vitro and in vivo. Vitamin E inhibited CA enzyme and the IC50 value of the vitamin was 0.039 mM in vitro. Similarly, it was seen that vitamin E inhibited CA enzyme activity after the first hour following vitamin E injections in vivo. The activities of CA in groups of trout given vitamin E injection were measured at 1, 3 and 5 h and the corresponding activities were found to be 772.7 ± 290.5 (P < 0.05), 1286.4 ± 378.2 and 1005.7 ± 436.1 enzyme units (EU) g Hb-1. The difference over the control was significant (P < 0.05) in the first hour and insignificant at 3 and 5 h (P ? 0.05). The activity of CA in the control, which did not contain vitamin E, was determined as 1597.7 ± 429.0 EU g Hb-1.

Rat lung antioxidant enzyme activities and their specific proteins during hyperoxia

1988 ◽  
Vol 65 (2) ◽  
pp. 797-804 ◽  
Author(s):  
L. S. Crouch ◽  
R. A. Prough ◽  
K. A. Kennedy ◽  
J. B. Snyder ◽  
J. B. Warshaw
Keyword(s):  
Enzyme Activity ◽  
Antioxidant Enzyme Activities ◽  
Oxidized Glutathione ◽  
Rat Lung ◽  
Fetal Rat ◽  
Fetal Rat Lung ◽  
Specific Proteins ◽  
Glucose 6 Phosphate Dehydrogenase

The hyperoxia-induced increases in the activity of lung glucose-6-phosphate dehydrogenase (G-6-P) and glutathione reductase (GR) after exposure of rats to greater than 97% O2 for 6 days were accompanied by equivalent increases in the amount of the respective immunoreactive proteins. Hyperoxia also increased lung glutathione (GSH) + oxidized glutathione (GSSG) content and the magnitude of this hyperoxic response of increased GSH + GSSG, G-6-P, and GR (maximal 1.3- to 1.8-fold) declined as a function of age during the first 3 wk of life. Fetal rat lung explants cultured 4 days in 95% O2 showed increased G-6-P and GR activity and increased levels of the specific proteins 1.5-fold those of explants at 2 days of culture. We conclude that the hyperoxic response of increased rat lung G-6-P and GR activity in vivo and in vitro involves not just alteration of enzyme activity but also specific increases in the proteins catalyzing the reactions.

In Vivo and In Vitro Debromination of Decabromodiphenyl Ether (BDE 209) by Juvenile Rainbow Trout and Common Carp

2006 ◽  
Vol 40 (15) ◽  
pp. 4653-4658 ◽  
Author(s):  
Heather M. Stapleton ◽  
Brian Brazil ◽  
R. David Holbrook ◽  
Carys L. Mitchelmore ◽  
Rae Benedict ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Common Carp ◽  
Decabromodiphenyl Ether ◽  
Juvenile Rainbow Trout ◽  
Bde 209

Metabolic importance of Na+/K+-ATPase activity during sea urchin development.

1997 ◽  
Vol 200 (22) ◽  
pp. 2881-2892 ◽  
Author(s):  
P Leong ◽  
D Manahan
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Sea Urchin ◽  
Sodium Pump ◽  
Sea Water ◽  
Strongylocentrotus Purpuratus ◽  
Lytechinus Pictus ◽  
Stimulation Of

Early stages of animal development have high mass-specific rates of metabolism. The biochemical processes that establish metabolic rate and how these processes change during development are not understood. In this study, changes in Na+/K+-ATPase activity (the sodium pump) and rate of oxygen consumption were measured during embryonic and early larval development for two species of sea urchin, Strongylocentrotus purpuratus and Lytechinus pictus. Total (in vitro) Na+/K+-ATPase activity increased during development and could potentially account for up to 77 % of larval oxygen consumption in Strongylocentrotus purpuratus (pluteus stage) and 80 % in Lytechinus pictus (prism stage). The critical issue was addressed of what percentage of total enzyme activity is physiologically active in living embryos and larvae and thus what percentage of metabolism is established by the activity of the sodium pump during development. Early developmental stages of sea urchins are ideal for understanding the in vivo metabolic importance of Na+/K+-ATPase because of their small size and high permeability to radioactive tracers (86Rb+) added to sea water. A comparison of total and in vivo Na+/K+-ATPase activities revealed that approximately half of the total activity was utilized in vivo. The remainder represented a functionally active reserve that was subject to regulation, as verified by stimulation of in vivo Na+/K+-ATPase activity in the presence of the ionophore monensin. In the presence of monensin, in vivo Na+/K+-ATPase activities in embryos of S. purpuratus increased to 94 % of the maximum enzyme activity measured in vitro. Stimulation of in vivo Na+/K+-ATPase activity was also observed in the presence of dissolved alanine, presumably due to the requirement to remove the additional intracellular Na+ that was cotransported with alanine from sea water. The metabolic cost of maintaining the ionic balance was found to be high, with this process alone accounting for 40 % of the metabolic rate of sea urchin larvae (based on the measured fraction of total Na+/K+-ATPase that is physiologically active in larvae of S. purpuratus). Ontogenetic changes in pump activity and environmentally induced regulation of reserve Na+/K+-ATPase activity are important factors that determine a major proportion of the metabolic costs of sea urchin development.

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