A new methodology was applied to the synthesis of new imidazolones and oxyazepine derivatives containing imidazo thiazole fused rings. Starting with 5-(4-bromo phenyl) imidazo (2, 1-b) thiazole, which was synthesized using the standard procedure, the Carbaldehyed group was introduced at position 6 of 5-(4-bromo phenyl) imidazo (2, 1-b) thiazole. Then, this 6-carbaldehyed derivative was condensed with different substituted aromatic amines to afford new Schiff bases. The latter were cyclized into new oxazepine and imidazolone derivatives by using phthalic anhydride and glycine, respectively. These new derivatives were characterized by using FT-IR, 1HHNMR, and 13CNMR spectra, as well as examined (evaluated) for anti-bacterial and anti-fungal a

This work deals with thermal cracking of heavy vacuum gas oil which produced from the top of vacuum distillation unit at Al- DURA refinery, by continuous process. An experimental laboratory plant scale was constructed in laboratories of chemical engineering department, Al-Nahrain University and Baghdad University. The thermal cracking process was carried out at temperature ranges between 460-560^oC and atmospheric pressure with liquid hourly space velocity (LHSV) equal to 15hr^-1.The liquid product from thermal cracking unit was distilled by atmospheric distillation device according to ASTM D-86 in order to achieve two fractions, below 220^oC as a gasoline fraction and above 220^oC as light cycle o

Amoxicillin 1 was treated with thiosemicarbazide and Phosphoryl chloride to obtain a new derivatives that contains 1,3,4-thiadiazole moiety 2. Schiff bases compounds were synthesized by the reaction of compound 2 with different aldehydes such as benzaldehyde and some substituted Benzaldehyde; p-hydroy, p-Chloro, p-Nitro, p-Dimethylamino, p-Methyl, p-Methoxy, p-Ethoxy to give compounds 3a-h. The obtained compounds have tested towards gram -ve and gram +ve bacteria. The compound shows good to moderate result towards the bacteria.

A first step in this research was to synthesize Schiff's bases(1-3)using an Amoxcilline intensification reaction with different aromatic aldehydes in absolute ethanol. In benzene and refluxing conditions,Schiff's bases were cyclized with succinic and Phthalic anhydride to give a new sequence of 1,3-oxazepine derivatives(4-6) and (7-9),respectively.The last step,cyclization reactions with sodium azide in THF solvent resulted in the formation of [10 and 11], which are supposed to be biologically significant.FT.IR, 1H-NMR and 13C-NMR (for compound 4,7,9, and 11),as well as melting points reported, were used to characterize these prepared compounds ,Bacillus (G+), Staphylococcus (G+), and E.Coli (G-)were screened against these compounds. . To i

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.