Browsing by Author "Arslan, O"

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Affinity To Some Inhibitors of Human Carbonic Anhydrase-1 and Bovine Carbonic Anhydrase
(Marcel dekker inc, 1996) Arslan, O; Kufrevioglu, OI
The carbonic anhydrase Isoenzymes employed here have been purifield in high yields by affinity chromatograpy using different affinity gels(Sepharose4B-L-tyrosine-Benzensulfonamide). Inhibition effect of 2-Substituted-1,3,4-Thiadiazole-5-Sulfonamides on human carbonic anhydrase-I (HCA-I) and bovine carbonic anhydrase (BCA) have been determined. It was found that inhibition effects of these compounds on BCA and CA-I were very great.
Bentonite-Supported Catalase
(Serbian Chemical Soc, 2005) Alkan, S; Ceylan, H; Arslan, O
The properties of the clay bentonite as a support for enzyme immobilization were studied using the enzyme catalase. Such an immobilization does not result in enzyme inactivation and constitutes a valuable method for immobilizing catalase at high ionic strength. The bentonite-supported catalase was characterized in terms of pH and ionic strength dependencies, thermal and storage stability and kinetic parameters. These studies indicate that bentonite is a valuable support for the simple adsorption of enzymes.
The Effects of Some Pesticites on the Activity of Liver and Erythrocyte Enzymes (In Vitro)
(Taylor & Francis inc, 1996) Celik, I; Camas, H; Arslan, O; Yegin, E; Kufrevioglu, OI
The effect of pomarsol (tetramethyltriurem disulphide), Benlate 1-(N-Butlycarbomoyl) 2-(Metoxycarboxamido)-bezimidazol, meothrin (alpha-cyanophenoxbenzyl 2.2.3.3.-tetramethyl cyclopropanecarbonylate), Imperator [alpha-cyano 3-phenoxybenzyl-cis, trans-3- (2.2-dichroinyl)-2.2- dimetil research on GOT, GPT (liver enzymes) and CA-I, CA-II (Human erythrocyt) BCA (Bovine erythrocyt). Among the chemicals meothrin, imperator, sumicidin were determined to have inhibitory effect, on bovine CA, human CA and GOT enzymes, but ineffective on GPT enzyme. The I-50 values of chemicals caused inhibition were determined by means of activity percentage [I] diagrams. The values were 3.2x10(-2) M, 3.5x10(-2) M, 2.7x10(-2) M for GOT respectively. The values of same chemicals were 5.8x10(-3) M, 1.00x10(-2) M, 1.22x10(-2) M for CA-I, and 7.11x10(-3) M, 2.68x10(-2) M, 1.22x10(-2) M for CA-II respectively on the order nand, these chemical were 9.25x10(-3) M, 8.65x10(-3) M and 1.63x10(-2) M for bovine CA.
Influence of Some Pesticides on Activity of Seven Serum Enzymes (In Vitro)
(Marcel dekker inc, 1997) Sekeroglu, MR; Celik, I; Arslan, O
The purpose of this study was to investigate the effects of Endosulfan [6,7,8,9, 10, 10-hexachloro- 1,5. 5a. 6, 9, 9 a hexahydro- 6, 5, methano - 2, 4, 3-benzo (e) dioxathpiepin 3- oxide], Mavrik [alpha-cyano -3-phenoxybenzyl M -(2 chloro-alpha-alpha-alpha-triflouro-p-tolyl)- D - valinate], 2,4-D (2,4-Dichlorophenoxyacetic acid) and Neoran (isopropyl -4,4-dibromobenzilate) on serum amylase (EC 3.2.1.1), creatine kinase (CK; EC 2.7.3.2) aspartate amino transferase (AST; EC 2.6.1.1), alanine aminotransferase (ALT; EC 2..6.1.2), alkaline phosfatase (ALP; EC 3.1.3.1), gamma glutamyl transferase (GGT; EC 2.3.2.2) and lactate dehydrogenase (LDH; EC 1.1.1.27). I-50 values of chemicals caused inhibition were determined by means of activity percentage -[I] diagrams. Endosulfan had effect of inhibition only on AST. The I-50 value of chemical was determined as 3.13x10(-4) M. Mavrik had effects of inhibition on AST, ALT, ALP and LDH. The values of I-50 were 7.83x10(-4) M, 1.17x10(-4), 1.23x10(-3) M and 2.23x10(-3) M, respectively. 2,4-D had effects of inhibition on ALT, ALP, GGT and LDH. The I-50 values of chemical were 6.97x10(-2) M, 5.05x10(-2) M, 2.35x10(-2) M, 1.07x10(-2) M, respectively. On the other hand, Neoran had effects of inhibition of all enzymes except amylase. I-50 values of this compound on other enzymes (CK, AST, ALT, ALP, GGT and LDH) were 4.41x10(-4) M, 5.06x10(-3) M, 2.40x10(-3) M, 5.23x10(-3) FA,4.4x10(-3) M, 5.97x10(-3) M, respectively.
The Inhibition Effects of Some Pesticides on the in Vitro Activity of Five Serum Enzymes
(Taylor & Francis inc, 1997) Arslan, O; Sekeroglu, R; Celik, J; Tarakci, M
The effect of some pesticides on alkaline phosphatase (ALK-P) (E.C 3.1.3.1), Amylase (E.C. 3.2.1.1) creatine kinase (CK) (E.C. 2.7.3.2), delta-glutamyltransferase (GGT-P) (E.C. 2.3.2.1) and lactate dehydrogenase (LDH) (E.C. 1.1.1.27) were investigated. These pesticides were baytroid [Cyano-(4-fluoro-3-phenoxyphenyl)-methly-3-(2,2-dichloroethenly)-2,2-dimetylcyclopropancarboxylate], imperator [cyano-3-phenoxy-benzyl-cis,trans-3-(2,2-dichloroethenyl)-2,2- dimetylcyclopropancarboxylate]. Meothrin [cyanophenoxybenzyl- 2,2, 3,3-tetramethyl cyclopropanecarboxylate], Sumicidin [cyano-3-phenoxybenzylcyclopropane carboxylate] T C A (trichloroacetic acid) and talstar. ISO values of chemicals caused inhibition were determined by means of activity percentage [I] diagrams. Pesticides having the strongest inhibitory effects on each enzyme were found to be talstar (I-50 = 7,3 x 10(-4) M) for ALK-P; talstar (I-50) = 7,1 x 10(-4) M) and baytroid (I-50 = 8.8 x 10(-4) M) For amylase; baytroid (I-50 = 1,25 x 10(-4) M) for CK. baytroid (I-50 = 8.8 x 10(-4) M and I-50 = 9,7 x 10(-4) M) for GGT-P and LDH. Baytroid and talstar In general caused a high inhibition for all enzymes. pollutants such as TCA, meothrin, imparator, sumicidin weakly inhibed each enzymes.
Polyphenol Oxidase From Allium Sp
(Amer Chemical Soc, 1997) Arslan, O; Temur, A; Tozlu, I
Polyphenol oxidase (PPO) was isolated from Allium sp. PPO showed activity to catechol and DL-dopa (K-m values were 25 mM for cathecol and 33 mM for DL-dopa; V-max values were 666 EU/mL . min for cathecol and 166 EU/mL . min for DL-dopa). Catechol was the most suitable substrate for Allium sp. PPO (lowest K-m value). The optimum pH for the PPO was 7.5 on substrates catechol and DL-dopa. Heat inactivation studies showed temperature >40 degrees C resulted in loss of enzyme activity. Heating for 30 min at 40 degrees C did not cause a significant loss of enzymatic activity. Allium sp. PPO was significantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, and sodium metabisulfide.
Polyphenol Oxidase From Malatya Apricot (Prunus Armeniaca L.)
(Amer Chemical Soc, 1998) Arslan, O; Temur, A; Tozlu, I
Polyphenol oxidase (PPO) of Malatya apricot was isolated by (NH4)(2)SO4 precipitation and dialysis. PPO showed activity to catechol, L-dopa, and gallic acid. Catechol was the most suitable substrate for Malatya apricot PPO (lowest K-m value). The optimum pH for the PPO was 8.5. Heating for 40 min at 40 degrees C did not cause a significant loss of enzymic activity. The times required for 50% inactivation of activitiy at 60 and 80 degrees C were found to be 47 and 16 min, respectively. The I-50 values of inhibitors studied on PPO were determined by means of activity percentage [I] diagrams. The values were 2.7 x 10(-5), 5.03 x 10(-5), 3.62 x 10(-5), 3.68 x 10(-5), and 8.30 x 10(-4) M for sodium metabisulfite, ascorbic acid, 2-mercaptoethanol, thiourea, and salicylic acid, respectively. Ascorbic acid, 2-mercaptoethanol, sodium metabisulfite, and thiourea inhibited the reaction strongly.
Substrate Specificity, Heat Inactivation and Inhibition of Polyphenoloxidase From Anethum Graveolens L
(Chiriotti Editori, 1997) Arslan, O; Tozlu, I
Polyphenoloxidase (PPO), isolated from Anethum graveolens L, showed activity on catechol, L-tyrosine and DL-DOPA. The optimum pH for the PPO was 7.0. Heat inactivation studies showed that heating for 40 and 15 min at 60 degrees and 80 degrees C, respectively, caused a 50% loss in enzymatic activity. The enzyme catalysed browning reaction was significantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, uric acid and barbituric acid. The most effective inhibitors were ascorbic acid and 2-mercaptoethanol.