The present study aims to detect CTX-M-type ESBL from Escherichia coli clinical isolates and to analyze their antibotic susceptibility patterns. One hundred of E. coli isolates were collected from different clinical samples from a tertiary hospital. ESBL positivity was determined by the disk diffusion method. PCR used for amplification of CTX-M-type ESBL produced by E. coli. Out of 100 E. coli isolates, twenty-four isolates (24%) were ESBL-producers. E. coli isolated from pus was the most frequent clinical specimen that produced ESBL (41.66%) followed by urine (34.21%), respiratory (22.23%), and blood (19.05%).  After PCR amplification of these 24 isolates, 10 (41.66%) isolates were found to possess CTX-M genes. The CTX-M type ESBL

The present study was carried out to determine the bacterial isolates and study their antimicrobial susceptibility in case of burned wound infections. 70 burn wound swabs were taken from patients, who presented invasive burn wound infection from both sex and average age of 3-58 years, admitted to teaching medical Al- Kendi hospital from October 2007 to June 2008. Pseudomonas aeruginosa was found to be the most common isolate (48.9%) followed by Staphylococcus aureus (24.4%), Citrobacter braakii (13.3%), Enterobacter spp. (11.1%), Coagulase-negative Staphylococci (11.1%), Proteus vulgaris (6.66%), Corynebacterium spp. (6.66%), Micrococcus (6.66%), Proteus mirabilis (4.44%), Enterococcus faecalis (4.44%), E.coli (4.44%), Klebsiella spp. (2.22

his study aims to determine most stable isobar from some isobaric elements with mass number (A= 50-65 & 180-195). This aim achieved by, firstly: plot mass parabolas for these isobaric family, second: calculated the atomic number for most stable isobar (ZA) value. To plot the mass parabola, the binding energy (B.E) calculated from semi empirical formula for these isobars. The mass number (A) plotted as a function to the (ZA) for each range; we get a linear relationship between them. An empirical formula for the most stable isobar has been developed from this linear dependence. From the results, we can see that mass parabolas for isobaric elements with odd mass number (A) are different from the mass parabolas of even mass number (A) isobars,

Removal of solar brown and direct black dyes by coagulation with two aluminum based
coagulants was conducted. The main objective is to examine the efficiency of these
coagulants in the treatment of dye polluted water discharged from Al-Kadhymia Textile
Company (Baghdad-Iraq). The performance of these coagulants was investigated through
jar test by comparing dye percent removal at different wastewater pH, coagulant dose,
and initial dye concentration. Results show that alum works better than PAC under acidic
media (5-6) and PAC works better under basic media (7-8) in the removal of both solar
brown and direct black dyes. Higher doses of PAC were required to achieve the
maximum removal efficiency under optimum pH co

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

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.