Abstract:
Eclipta alba is a weed growing in damp, moist puddles distributed in the tropical and subtropical regions, so the most weight of the plant is water, which reached in to 90%. The extraction method by using different solvents (Methanol, Ethanol, Hexane and Aqueous) showed, the best yield with methanol reached to 76%, and the yield decreased with ethanol and hexane reached 55% and 53% respectively, while the minimum yield observed with aqueous hot and cold extraction reached 11% and 5% respectively. The phytochemical compound characterization showed the compounds (Coumarines , Flavones ,Volatile Oil ,Tannins , Saponines , Glycosides ,Carbohydrates ,Alkaloids , Resins) with different percentage. The thin layer chromatography det

Introduction: Melanin is a high-molecular weight pigment produced through the oxidative polymerization of phenolic or indolic compounds and plays a perfect role in UV-light shielding, as well as in photoprotection. Among biopolymers, melanin is unique in many aspects. This study is designed to screen Production, extraction and characterizes of an extracellular melanin pigment from clinically isolated P. aeruginosa. Objective: The aim of the current study is isolation and diagnosis of P.aeruginosa using vitek-2 compact system and screening the ability to produce melanin and characterization of extracted melanin by UV-vis, FTIR, XRD and SEM. Materials and methods: the samples swab inoculated on cetrimide agar as selective media and incubated

Ninety five samples were collected from different samples (urine, ear and wounds swaps), from hospitals in Baghdad city. The results of cultural, microscopic , biochemical tests indicated that in urine samples E.coli have high occurrence frequency 19 (47.5%) followed by Proteus mirabilis 18(45%) and Klebsiella species 1 (2.5%), while in wounds samples each of Pseudomonas spp. and Proteus mirabilis 10 (25%) , then followed by E.coli with 5 (12.5%) and Klebsiella species 3 (7.5%). Ear swaps samples revealed that Pseudomonas aeruginosa 7 (46%) was the major bacterium followed by Proteus mirabilis 4(26.6).Sensitivity test against eleven antimicrobial agents was done for all of the Proteus mirabilis isolates (32 isolates). The results display

This study includes adescription of Human serum Albumin by amodified using ion- exchange chromatography with manipulated comparison with cold ethanol precipitation method , It has been nticed that this procedure is superior orer the classical method . The Final yield by the new method 69.32% with purity of 83.42% compared with cohn which yield 60.30 % with purity of 80.7 % . The new method prored that it suitable for the pusi Fication of such material because it yield no precipitation material and it increases the Final yield of albumin solutions . • Human serum Albumin . • Albumin purification . • Ion – exchange chromatography . • Human plasma . • Albumin extraction .

Catalase (EC 1.11.1.6) is a well known enzyme which exists in almost all living creatures exposing to oxygen (such as plants, bacteria, and animals). It is a very necessary enzyme to protect the cell from oxidative detriment by reactive oxygen species (ROS). The aim of this study is the partial purification and characterization of Catalase enzyme from Banana peels. In this study, fresh banana peels are treated with 70 % ethanol ,further separated with chloroform ,water and ethyl acetate respectively .The supernatant of the enzymatic sample which is treated with chloroform is loaded into gel filtration column with Sephadex G-100 (1.0 x 90 cm) equilibrated with pH7 buffer media (phosphate buffer 0.1 M). Kinetic studies of the purified en

From 211 urine samples, Gram negative bacteria were isolated from only 61 urine samples with isolation percentage 28.9%. Escherichia coli were isolated percentage 70.49% while Klebsiella pneumoniae and Psendomonas aeruginosa were 8.19% and 6.55%, respectively.Proteus spp. Were isolated from 9 (14.75%), P. mirablis and P. vulgaris were isolates percentage 11.47% and 3.27%, respectively. Uroepithelial Cell Adhesin (UCA) fimbriae expression by P.mirabilis isolates was detected by the high capacity to adhesion to human uroepithetial cells, the isolate p.mirabilis U7 was adhesion to human uroepithelial cells mean no.30.2 bacteria/cell when grown on luria broth at 37C for 24h, but then grown it’s on luria agar at 37C for 24h the adhesion

Lipoxygenase was extracted from the cup of Pleurotus ostreatus ( Jaq : Fr ) oyster mushroom for the first time in Iraq, and purified homogeneously through precipitation with 40% saturation of (NH4)2SO4 as a partial purification then loaded on DEAE-Cellulose (Diethyl amino ethyl Cellulose) ion-exchange chromatography column and then the highly active elution parts have been passed through gel filtration column with Sephacryl S-300 as a final purification with 804 (U/mg protein) specific activity, 11.32 fold of purification and 36.54% yield . The molecular weight of the enzyme was estimated to 74 KDa by gel filtration Sephacryl S-300 column and the isoelectric point for enzyme was 5.3. The optimal pH for lipoxygenase activity and stability

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attai

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