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Mohammad Hakimelahi,Mohammad Reza Alavi Moghaddam,Seyed Hossein Hashemi 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.4
The performance of one stage anaerobic/aerobic processes for the biological treatment of synthetic wastewaters containing Acid Red 18 was studied. In addition, a method for evaluating dye mineralization using lumped parameters was investigated. The selected initial dye concentrations were 0, 35, 70, 140, and 280 mg/L, in reactors R1 ~ R5,respectively. This study showed that average COD removal was not lower than 85% while the remaining COD originated from Acid Red 18 and its degradation products. The majority of the dye removal occurred in the anaerobic phases and the aerobic phase contributions were insignificant. The kinetics data of dye removal showed that the increase in initial dye concentration (35 ~ 280 mg/L) caused a decrease in first-order kinetic rate constants (0.0593 ~ 0.0384/h). The overall mineralization of AR 18 dye was at least 44,35, 13, and 0% in R2 ~ R5, respectively. Increase in initial dye concentrations had no significant effect on sludge characteristics.
A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
Saboury, Ali Akbar,Divsalar, Adeleh,Jafari, Ghasem Ataie,Moosavi-Movahedi, Ali Akbar,Housaindokht, Mohammad Reza,Hakimelahi, Hosain 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at $27^{\circ}C$ using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to $140\;{\mu}M$ by the microcalorimetry method, which agrees well with the value of $143\;{\mu}M$ for the inhibition constant that was obtained from the spectroscopy method.
Modification of Substrate Inhibition of Synaptosomal Acetylcholinesterase by Cardiotoxins
Ranaei-Siadat, Seyed-Omid,Riazi, Gholam-Hosein,Sadeghi, Mehdi,Chang, Long-Sen,Lin, Shinne-Ren,Eghtesadi-Araghi, Peyman,Hakimelahi, Gholam Hossein,Moosavi-Movahedi, Ali Akbar Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.3
Different types of cardiotoxin (I-V and n) were isolated and purified from the venom of the Taiwan cobra (Naja naja atra). The effects of these cardiotoxins were studied on membrane-bound acetylcholinesterase, which was isolated from a sheep's brain cortex. The results showed that cardiotoxins I-III, V, and n activated the enzyme by modification of substrate inhibition, but cardiotoxin IV's reaction was different. The inhibition and activation of acetylcholinesterase were linked to the functions of the hydrophobicity index, presence of a cationic cluster, and the accessible arginine residue. Our results indicate that Cardiotoxins have neither a cationic cluster nor an arginine residue in their surface area of loop I; therefore, in contrast to fasciculin, cardiotoxins are attached by loop II to the peripheral site of the enzyme. As a result, fasciculin seems to stabilize nonfunctional conformation, but cardiotoxins seem to stabilize the functional conformation of the enzyme. Based on our experimental and theoretical findings, similar secondary and tertiary structures of cardiotoxins and fasciculin seem to have an opposite function once they interact with acetylcholinesterase.
A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
(Ali Akbar Saboury),(Ghasem Ataie Jafari),(Ali Akbar Moosavi Movahedi),(Mohammad Reza Housaindokht),(Gholam Hosain Hakimelahi),(Adeleh Divsalar) 생화학분자생물학회 2002 BMB Reports Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at 27oC using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 140 μM by the microcalorimetry method, which agrees well with the value of 143 μM for the inhibition constant that was obtained from the spectroscopy method.
Modification of Substrate Inhibition of Synaptosomal Acetylcholinesterase by Cardiotoxins
( Seyed Omid Ranaei Siadat ),( Gholam Hosein Riazi ),( Mehdi Sadeghi ),( Long Sen Chang ),( Shinne Ren Lin ),( Peyman Eghtesadi Araghi ),( Gholam Hossein Hakimelahi ),( Ali Akbar Moosavi Movahedi ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.3
Different types of cardiotoxin (I-V and n) were isolated and purified from the venom of the Taiwan cobra (Naja naja atra). The effects of these cardiotoxins were studied on membrane-bound acetylcholinesterase, which was isolated from a sheep`s brain cortex. The results showed that cardiotoxins I-III, V, and n activated the enzyme by modification of substrate inhibition, but cardiotoxin IV`s reaction was different. The inhibition and activation of acetylcholinesterase were linked to the functions of the hydrophobicity index, presence of a cationic cluster, and the accessible arginine residue. Our results indicate that Cardiotoxins have neither a cationic cluster nor an argininge residue in their surface area of loop I; therefore, in contrast to fasciculin, cardiotoxins are attached by loop II to the peripheral site of the enzyme. As a result, fasciculin seems to stabilize nonfunctional conformation, but cardiotoxins seem to stabilize the functional conformation of the enzyme. Based on our experimental and theoretical findings, similar secondary and tertiary structures of cardiotoxins and fasciculin seem to have an opposite function once they interact with acetylcholinesterase. s