The ligand 4-(2-aminmo-5-nitro-phenylazo)-1,5-dimethyl-2-phenyl-1,2-dihydro-pyrazol-3-one derived from 4-aminoantipyrine and 4-nitroaniline was synthesized. The synthesized ligand was characterized by 1HNMR, FT-IR, UV-Vis spectra and (C.H.N) analysis. Complexes of (YIII and LaIII ) with the ligand were prepared in aqueous ethanol with a 1:2 M:L ratio and at optimum pH. The prepared complexes were characterized by using flame atomic absorption, FT-IR, UV-Vis spectra,(C.H.N) analysis and conductivity measurement. The stoichiometry of complexes was studied by the mole ratio and job methods. A concentration range (1×10-4 - 3×10-4 M) obeyed Beer's law, the complex solutions show high values of molar absorption. On the basis of physicochemical

The ligand 4-(2-aminmo-5-nitro-phenylazo)-1,5-dimethyl-2-phenyl-1,2-dihydro-pyrazol-3-one derived from 4-aminoantipyrine and 4-nitroaniline was synthesized. The synthesized ligand was characterized by 1HNMR, FT-IR, UV-Vis spectra and (C.H.N) analysis. Complexes of (YIII and LaIII ) with the ligand were prepared in aqueous ethanol with a 1:2 M:L ratio and at optimum pH. The prepared complexes were characterized by using flame atomic absorption, FT-IR, UV-Vis spectra,(C.H.N) analysis and conductivity measurement. The stoichiometry of complexes was studied by the mole ratio and job methods. A concentration range (1×10-4 - 3×10-4 M) obeyed Beer's law, the complex solutions show high values of molar absorption. On the basis of physicochemical

Proteinases (E.C.3.4.21) family are widely distributed in the nature; it was present in animals tissues , plants and microbial cell . Protease was purified from Zahdi seed (Phoenix dactylifera L.) by several steps included ammonium sulphite ppt (75%) saturation and dialyzed against the 80mM sodium phosphate buffer at pH 7.5 . The enzyme specific activity was 407.62 unit/mg protein. The obtained extract was purified by DEAE-Cellulose column followed by gel filtration through Sephacyl S-200 column .The enzyme specific activity ,yield and purification fold were 1873.49 unit/mg protein, 22.99 and 58.42% respectively. The results of protease characterization showed that the molecular weight was 25118 daltons as determined by gel f

  Diazotization reaction between quinolin-2-ol and (2-chloro-1-(4-(N-(5-methylisoxazol-3-yl)sulfamoyl)phenyl)-2l4-diazyn-1-ium was carried out resulting in ligand-HL, this in turn reacted with the next metal ions (Ni2+, Pt4+, Pd2+, and Mn2+)  forming stable complexes with unique geometries such as (tetrahedral for both Ni2+ and Mn2+, octahedral for Pt4+ and square planer for Pd2+ ). The creation of such complexes was detected by employing spectroscopic means involving ultraviolet-visible which proved the obtained geometries, fourier transfer proved the formation of azo group and the coordination with metal ion through it. Pyrolysis (TGA & DSC) studies proved the coordination of water residues with metal ions inside the coordin

Diazotization reaction between quinolin-2-ol and (2-chloro-1-(4-(N-(5-methylisoxazol-3-yl)sulfamoyl)phenyl)-2l4-diazyn-1-ium was carried out resulting in ligand-HL, this in turn reacted with the next metal ions (Ni²⁺, Pt⁴⁺, Pd²⁺, and Mn²⁺)  forming stable complexes with unique geometries such as (tetrahedral for both Ni²⁺ and Mn²⁺, octahedral for Pt⁴⁺ and square planer for Pd²⁺ ). The creation of such complexes was detected by employing spectroscopic means involving ultraviolet-visible which proved the obtained geometries, fourier transfer proved the formation of azo group and the coordination with metal ion through it. Pyrolysis (TGA &

RKASFH Ghanim, Ibn Al -Haitham Journal for pure and applied science, 2017

Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a

     New chelating ligand derived from triazole and its complexes with metal ions Rhodium, Platinum and Gold were synthesized. Through a copper (I)-catalyzed click reaction, the ligand produced 1,3-dipolar cycloaddition between 2,6-bis((prop-2-yn-1-yloxy) methyl) pyridine and 1-azidododecane. All structures of these new compounds were rigorously characterized in the solid state using spectroscopic techniques like: 1HNMR, 13CNMR, Uv-Vis, FTIR, metal and elemental analyses, magnetic susceptibility and conductivity measurements at room temperature, it was found that the ligand acts as a penta and tetradentate chelate through N3O2, N2O2, and the geometry of the new complexes are identified as octahedral for (Rh & Pt) complexes a

     New chelating ligand derived from triazole and its complexes with metal ions Rhodium, Platinum and Gold were synthesized. Through a copper (I)-catalyzed click reaction, the ligand produced 1,3-dipolar cycloaddition between 2,6-bis((prop-2-yn-1-yloxy) methyl) pyridine and 1-azidododecane. All structures of these new compounds were rigorously characterized in the solid state using spectroscopic techniques like: ¹HNMR, ¹³CNMR, Uv-Vis, FTIR, metal and elemental analyses, magnetic susceptibility and conductivity measurements at room temperature, it was found that the ligand acts as a penta and tetradentate chelate through N₃O₂, N₂O₂, and the geometry of the new complex