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bsj-1027
Purification and Characterization of protease from Zahdi dates plam seeds (Phoenix dactylifera L.)
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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 filtration. The optimum temperature of the enzyme activity 35 C for 15 minutes and that for stability was 45 C for 15 minutes, using sodium phosphate buffer at pH 7.5, The optimum pH for the enzyme stability and activity were 8.5 for 15 minute and 7.5 respectively.

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Publication Date
Sun Mar 13 2011
Journal Name
Baghdad Science Journal
Effect of Phoenix dactylifera pollen grains suspension on spermatogenesis and some biochemical parameters in albino rats
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In this study forty mature albino rats were used wich were randomly divided into five groups ,four groups were adminstrated Phoenix dactylifera pollen grains suspension at concertenrations (18,54,108,and 216)mg/ kg body weight by oral administration while the fifth group was considered as a control group.Experiment continued for 40 days then rats were sacrificed and samples of blood were collected for determination of some biochemical parameters (total protein ,total cholesterol ,LDLc and HDLc).Testis were removed for preparation histological sections to measures the diameters of seminferous tubules ,thickness of seminiferous epithelium and the numbers of spermatogenic cells.

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Publication Date
Sun Jan 01 2023
Journal Name
Journal Of Population Therapeutics And Clinical Pharmacology
Purification and Characterization of Antifungal Protein from Bacteria
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Publication Date
Thu May 25 2017
Journal Name
Ibn Al-haitham Journal For Pure And Applied Sciences
Physiochemical and Spectral Characterization For a Biological Active, Solanidine&Solasodine Partial Purification Compounds From (Solanum nigrum L)
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 This study includes a physiochemical and a spectrocpical characterization to some alkaloid compounds in the (ANAB AL- THEAB) plant (Solanum nigrun L.). It’s the most important medicinal herb belonging to the family (Solanaceae). Acid  hydrolysis was performed by using limited conc. of  Hcl and H2SO4, to obtain the aglycon  part of previously separated steroidal componants as (A, B and C).   The characterization of the(A,B and C) compounds indicates that they varied between them as the separated steroidal like-alkaloids, carried by using melting  point (m.p.), thin layer chromatography (TLC), Infra -Red  spectroscopy (IR) and Ultra violet-Visible  spectroscopy (UV - Visible).High perfor

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Publication Date
Sun Jun 01 2014
Journal Name
Baghdad Science Journal
Partial purification and characterization of xylanase from Bacillus cereus X3
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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

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Publication Date
Sun Mar 01 2009
Journal Name
Baghdad Science Journal
Purification and Characterization β - lactamase produce from local isolate Klebsiella pneumonia
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Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.

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Publication Date
Sun Mar 13 2011
Journal Name
Baghdad Science Journal
Extraction and purification of L-Asparaginase II from local isolate of Proteus vulgaris
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Forty one isolates of genus Proteus were collected from 140 clinical specimens such as urine, stool, wound, burn, and ear swabs from patients of both sex. These isolates were identified to three Proteus spp. P. mirabilis, P. vulgaris and P. penneri .The ability of these bacteria to produce L-asparaginase II by using semi quantitative and quantitative methods was determined. P. vulgaris Pv.U.92 was distinguished for high level of L-asparaginase II production with specific activity 1.97 U/mg. Optimum conditions for enzyme production were determined; D medium with 0.3% of L-asparagine at pH 7.5 with temperature degree 35°C for incubation. Ultrasonication was used to destroy the P. vulgaris Pv.U.92 cells then ASNase II was extracted and pu

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Publication Date
Sun Sep 01 2013
Journal Name
Baghdad Science Journal
Purification and Characterization of Endoglucanase from local isolate of Aspergillus flavus
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Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

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Publication Date
Sun Dec 02 2012
Journal Name
Baghdad Science Journal
Effect of Aqueous and Ethanolic Extracts of Tribulus terrestris, Phoenix dactylifera and Nasturtium officinale Mixture on Some Reproductive Parameters in Male Mice
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The present investigation was conducted to evaluate the effect of the crude extracts mixture of three plants (Tribulus terrestris, Phoenix dactylifera and Nasturtium officinale) on semen quality,sex hormones and reproductive performance of mature male mice. A group of 25 male mice given 150mg/kg/day of the powder of the plants mixture with the food for four weeks and another three groups of 25 animals each given intraperitoneal injection from each of the aqueous and ethanolic extracts with a doses 75, 150, and 300mg/kg/day for two weeks. A remarkable increase in sperm concentration and motility with a decreased abnormal morphology was obtained in the experimental groups. A significant increase in hormones level were recognized in most grou

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Publication Date
Thu May 25 2017
Journal Name
Ibn Al-haitham Journal For Pure And Applied Sciences
Purification, Characterization and Antifungal Activity of Chitinase from Serratia marcescens Isolated from Fresh Vegetables
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  Seven [35%] and five [25%] Serratia marcescens  isolates were obtained out of 20 samples of lettuce and 20 samples of spinach, respectively, taken from different locations in a farm in Baghdad city. The isolate that produced chitinase in higher level was chosen to purify chitinase through several stages of purification including: ammonium sulfate precipitation, DEAE- sephadex ion exchange chromatograpgy and sephadex G-200 gel filtration with 89.5- fold purification and 30% recovery.       The purified chitinase was characterized and the molecular weight of enzyme was 59000 daltons by using gel filtration chromatography. The optimum pH and temperature of the purified chitinase were 6.0 and 50°

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Publication Date
Thu Jan 01 2015
Journal Name
Iraqi Journal Of Science
Production, Purification and Characterization of Cellulose from Local Isolate of Pantoea spp
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