Recently, Systemic lupus erythematosus (SLE) was considered as one of the autoimmune diseases that the genetic and environmental factors contributed in the disease etiological profile. According to the environmental factors, infectious agents have been concluded to have a role in the etiology and pathogenesis of SLE. Chlamydia pneumoniae and Mycoplasma pneumoniae are among these infectious agents that have been suggested to be involved in the etiology of SLE. Accordingly, the current study was designed to assess the anti-C. pneumoniae and anti-M. pneumoniae IgG antibody status by enzyme linked immunosorbent assay (ELISA) in the sera of 64 Iraqi SLE females' patients and 32 Iraqi healthy females as controls. The patients' group were distribu

A simple low-cost approach at various exposure times was utilized to generate cold plasma in the aim to fabricate AuNPs. UV-Visible spectra and X-ray diffraction were used to characterize the nanoparticles (XRD). Surface Plasmon resonance was observed in the synthesized AuNPs at 530, 540, and 533 nm. For all samples, the patterns of XRD show very intensive peaks implying the fcc crystalline structure of AuNPs. The average crystallite size of AuNPs is ranging between 20-30 nm. The observation of morphology by FESEM revealed the spherical formation of AuNPs. Doses of 100 and 200 ppm of AuNPs were adapted to investigate their effect on the blood-mixture with and without a 20-second of cold plasma exposure. The WBC components in the blood

The purpose of this study is to determine the useful of Schiff bases derivatives containing (oxazepine, tetrazole) rings with biological activity which can be used as drug and antimicrobial, the present work is started from [Binary (2,5(4,'4-diaminophenyl) – 1,3,4 – oxadiazole]. A variety of Schiff bases and heterocyclic (oxazepine, tetrazole) have been synthesis, and confirm that structures by physical properties , FTIR , 1H-NMR, 13C-NMR, elemental analysis, [Microbial study against three type of bacteria (staphylococcus aurea and klebsiella pneumonia) and (Canadida albncans) fungi].All analyzation performed in center of consulatation University of Jordan.

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

The study aimed to purification of acid phosphatase (ACP) from sera of obesetype 2 diabetes mellitus patients, this study included from thirty T2DM patients and thirty control, purification process was done with several steps included precipitation with inorganic salt (NH4 ) 2SO4 30%-80%, dialysis, ion exchange chromatography by DEAE sepharose anion column and size exclusion chromatography by Sepharose 6B.ACP, BMI, FBS, HbA1c, Lipid profile, Urea, Creatinie, Insuline, Homa-IR were determined. Results showed the precipitate and concentrated protein appeared four peaks in ion exchange column. ACP located in the first and second peak with purification fold (21.1), (37.2) yield of enzyme and specific activity (173.3) IU/ml, which obtained a si

: Partial purification of phosphoenolpyruvate carboxykinase (PEPCK) from type 2 diabetic patients sera take place using some purification steps such as participation with ammonium sulphate (55-80%) and filtered through dialysis, then ion exchange chromatography by DEAE sepharose anion column, gel filtration chromatography by sephadex G-100 column. In ion exchange step, there are four peak are obtained, the highest enzyme activity obtained by (0.4 M Nacl) with purification fold (2.18), yield (44.3) of enzyme and specific activity (13.5) mg/ng, which obtained a single peak by gel filtration chromatography, the degree of purification (5.34) fold, yield of enzyme (20%) with specific activity (33.109mg/ng). The purified enzyme had an optimum tem

This study was performd on 50 urine specimens of patients with type 2 diabetes, in addition, 50 normal specimens were investigated as control group. The activity rate of maltase in patients (6.40±2.17) I.U/ml and activity rate of maltase in normal (0.44±0.20)I.U/ml. The results of the study reveal that maltase activity of type 2 diabetes patient's urine shows significant increase (P<0.01) compare to normal.

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

An extracellular β-galactosidase from the thermophilic fungus Rhizomucor
Pusillus IB8 has been purified via several steps included precipitation by ammonium
sulphate at 80 % saturation, DEAE- Cellulose Ion exchange chromatography and gel filteration on sepharose CL-6B column. The Final purification folds and the yield of the enzyme were 42.5 and 24.8 % respectively. The purified β-galactosidase has an optimum pH for its activity between 4.5 to 5, while the optimum pH for enzyme stability was between 5 to 5.5. Futhermore, it was found that the optimum temperature for its activity was 60 C°. The purified enzyme retained approximatly 98% of its original activity when incubated at 60 C° for 60 min. However, 25 % of its activity was