Browsing by Author "Turkoglu, V"

Now showing 1 - 3 of 3

Effects of Neostigmine Methylsulfate on Enzyme Activity of Acetylcholinesterase in Rat Serum, Plasma, Muscle and Liver in Vivo
(Scandinavian Federation Laboratory Animal Science, 2005) Demir, H; Turkoglu, V
This study was designed to investigate the effects of neostigmine methylsulfate oh enzyme activity of acetylcholinesterase (AChE) in rat serum, plasma, muscle and liver were investigated in vivo. Twelve Sprague-Dawley Albino male rats, weighing 150-200 g were housed in two groups, each group containing six rats. A single dose (0.05 mg/kg) of neostigmine methylsulfate was injected intramuscularly to the treatment rats. Control rats were given only the same amount of physiological saline. Blood samples for enzyme activity were obtained by cardiac puncture under ether anesthesia one, three, and six hours after the treatment. The tissues were dissected six hours after the treatment. The present study indicated that neostigmine methylsulfate possessed an inhibitory effect on AChE activity in serum, plasma, muscle and liver with the elapse of time. However, the greatest inhibition was found six hours after the injection.
Effects of Some Antibiotics on Glucose 6-Phosphate Dehydrogenase in Sheep Liver
(Czech Academy Agricultural Sciences, 2002) Çiftçi, M; Turkoglu, V; Aldemir, S
In vitro effects of penicillin, sulbactum, cefazolin, and amikacine on the activity of the enzyme glucose-6-phosphate dehydrogenase in sheep liver were investigated. Glucose 6-phosphate dehydrogenase was purified from sheep liver, using a simple and rapid method. The purification consisted of two steps, preparation and homogenate and 2'.5'-ADP Seprarose 4B affinity chromotography. As a result of the two consecutive procedures, the enzyme, having the specific activity of 11.76 EU/mg proteins, was purified with a yield of 35.72% and 11.913 fold. In order to control the enzyme purification SDS polyacrylamide gel electrophoresis (SDS-PAGE) was done. SDS-PAGE showed a single band for the enzyme. In addition , I-50 values of the antibodies were determined by plotting activity % vs. antibiotic concentration. I-50 values were 17.71 mM for penicillin, 27.38 mM for sulbactum, 28.88 mM for cefazolin, and 30.59 mM for amikacine.
Purification and Characterization of Acetylcholinesterase From the Lake Van Fish (Chalcalburnus Tarichii Pallas, 1811)
(Taylor & Francis inc, 2003) Aliriz, S; Turkoglu, V
In this study, acetylcholinesterase (AChE; EC 3.1.1.7) was purified from plasma and erythrocytes in the Lake Van fish (Chalcalburnus tarichii P. 1811) by affinity chromatography. Enzymatic activity was spectrophotometrically measured according to Ellman's method, at 412 nm. Then, the optimal pH and temperature of the enzyme was determined. According to the results, the optimal pH and the optimum temperature were 8.0 and 25degreesC, respectively. In order to control the purification of the enzyme, sodium dodecyl-sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was done. SDS-PAGE showed a single band for enzyme. The purification rates for plasma AChE and erythrocyte AChE are 3251.6 and 8500, respectively.