The new Azo ligand and its metal complexes have been prepared and characterized The reaction of 4-nitroaniline and 2-hydroxy-1-naphthaldehyde in a 1: 1 mole ratio resulted in the synthesis of ((E)-2-hydroxy-3-((4-nitrophenyl) diazenyl)-1-naphthaldehyde)(HL). The separation of monomeric complexes was accomplished by reacting ((E)-2-hydroxy-3-((4-nitrophenyl) diazenyl)-1-naphthaldehyde)(HL) with Cr, Mn II, Co II, Ni II, and Cu II metal ions in a mole ratio of 2: 1 (L: M). Elemental microanalysis, magnetic susceptibility, conductance, FT-IR, electronic spectra, and 1 HNMR, 13 C-NMR, and mass spectra were among the analytical and spectroscopic techniques used to describe the products. Based on the data collected during the characterization process, six coordinates were determined. The ligand and its complexes were tested against certain bacteria and fungi. The findings acquired suggested that the metal complexes are more active against a variety of organisms have been studied as compared to the free ligand.
Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and BC
... Show MoreCholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and B
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Twelve N-(6-sustirured benzothanol-2-y1) succinamic acids and 3-(6-substitted benzonathol-2-y1)-carbamoyl propionyl chloride were synthesized in good yields from reaction of benzonathol2-yl)
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In this study the prevalence of acute, sub-acute and chronic toxoplasmosis were monitored in a group of Iraqi pregnant women according to the anti-T.gondii antibodies (IgG and IgM), as well as the levels of both progesterone and estrogen hormones were measured using mini-VIDAS®technique. This study demonstrated that there was high prevalence of chronic toxoplasmosis (31.70%) when it compared with acute and sub-acute type, results also showed that the acute toxoplasmosis always related with low concentration of both progesterone and estrogen which were (5.35 ± 7.15 ng/ml) and (70.66 ± 51.08 pg/ml) respectively