http://localhost:80/xmlui/handle/123456789/19284 2026-04-23T00:19:07Z 2026-04-23T00:19:07Z ALI, MUHAMMAD SHAIQ GHAFOOR AHMED PERVEZ, MUHAMMAD KASHIF MEHREEN LATEEF NIGHAT AFZA LUBNA IQBAL http://localhost:80/xmlui/handle/123456789/19806 2023-10-06T05:51:23Z 2011-12-20T00:00:00Z

Title: allo-Imperatorin: A Potent Urease Inhibitor from Fresh Unripe Fruits of Aegle marmelos (Rutaceae) Authors: ALI, MUHAMMAD SHAIQ; GHAFOOR AHMED; PERVEZ, MUHAMMAD KASHIF; MEHREEN LATEEF; NIGHAT AFZA; LUBNA IQBAL Abstract: During the search for bioactive constituents from different parts of Aegle marmelos (Rutaceae), the ethanol soluble portion of fresh unripe fruits yielded two known amides named aegeline (1) and 2-O-methyl aegeline (2), and five known coumarins named xanthotoxol (3), alloimperatorin (4), marmesin (5), marmin (6), 7′-O-methylmarmin (7). Structures of 1-7 were elucidated with the aid of spectroscopic techniques. All the isolated constituents (1-7) were tested for urease inhibition. allo-Imperatorin was found the most potent among the all tested samples with the IC₅₀ value 27.5 µM.

2011-12-20T00:00:00Z M. RASUL, JAN JASMIN SHAH KHADIM HUSSAIN SHAHNAZ PERVEEN KHAN, KHALID MOHAMMED ZAHID HUSSAIN http://localhost:80/xmlui/handle/123456789/19805 2023-10-06T05:49:42Z 2011-12-20T00:00:00Z

Title: Comparison of the Catalytic Activity of the Commercially Available Clays for the Conversion of Waste Polyethylene into Fuel Products Authors: M. RASUL, JAN; JASMIN SHAH; KHADIM HUSSAIN; SHAHNAZ PERVEEN; KHAN, KHALID MOHAMMED; ZAHID HUSSAIN Abstract: The use of clays as catalyst for the cracking of polyethylene was investigated and commercially available clays like China clay, Fuller’s earth and French chalk were used to convert polyethylene into fuel oil and fuel gas in addition to the wax. The conditions for the process were optimized for the china clay and the activities of other clays were investigated under same conditions. The activity of the clays was compared in terms of the amount of the products of the pyrolysis which include oil, wax and gas. The wax and oil were separated into its components using gas chromatograph equipped with FID. In the liquid sample the major components had the boiling points in the range of 125-180 °C. In case of the wax the same range of the compounds were observed with greater concentration of the high boiling point compounds. This wax can be used as feedstock for the oil industry. The cracking products were also characterized by various spectral and chemical tests. According to these investigations the products were identified as alkanes, alkenes and aromatics.

2011-12-20T00:00:00Z MEHRIN SHERAZI RUBINA NAZ ASMA SAEED AISHA SIDDIQUA SHAZIA AMEEN AHMAD SAEED http://localhost:80/xmlui/handle/123456789/19804 2023-10-06T05:47:54Z 2011-12-20T00:00:00Z

Title: Camel Liver Acid Phosphatases: Purificaion and Properties Authors: MEHRIN SHERAZI; RUBINA NAZ; ASMA SAEED; AISHA SIDDIQUA; SHAZIA AMEEN; AHMAD SAEED Abstract: Three acid phosphatases were identified from the liver of a camel. Of these, two high molecular weight acid phosphatase forms were isolated and purified by successive chromatography on SP-Sephadex C-50, Sephadex G-75, CM-Cellulose, Sephacryl HR-200 and Reactive Blue 4Agarose columns. These were designated as P-I and P-II. The acid phosphatase, P-I was purified to homogeneity. A 1200 times purification was obtained with specific activity of 17U/mg of protein and a total yield of 3%. The SDS-PAGE showed a single band corresponding to the molecular weight of 66 kDa. Electrophoresis of the native enzyme resolved a single protein band that migrated to approximately 130 kDa, indicating the dimeric nature of protein. The acid phosphatase, P-II was purified 1000-fold with specific activity of 15 U/mg of protein and recovery of 1%. The SDS-PAGE revealed a single band around 48-50 kDa. Gel filtration chromatography estimated a native molecular mass to be 100 kDa. Thus, high molecular weight acid phosphatases likely function as a homodimer, consisting of two similar subunits. Low molecular weight acid phosphatase as P-III, was purified 3000-fold with specific activity of 45 U/mg of total protein and was found homogeneous on SDS-PAGE. Molecular weight of 18 kDa was obtained. The P-I, P-II and P-III enzymes were the most active over pH range 4.8-6.0 and at 55°C. The pH stability was found between pH 4 and 9 and appeared to be stable at temperature of 40°C. The Km values were found to be 0.31, 0.27 and 0.16 mM, respectively. These were further characterized with respect to thermal inactivation, inhibition, purine activation, substrate specificity and other kinetic parameters.

2011-12-20T00:00:00Z OZTURKCAN, S. ARDA KADIR TURHAN ZUHAL TURGUT http://localhost:80/xmlui/handle/123456789/19803 2023-10-06T05:46:36Z 2011-12-20T00:00:00Z

Title: Synthesis and Characterizations of New 1,3-Oxazine Derivatives Authors: OZTURKCAN, S. ARDA; KADIR TURHAN; ZUHAL TURGUT Abstract: In this study, Betti's classical procedure, a Mannich-type aminoalkylation reaction of 2- naphthol with various aldehydes was applied in the presence of ammonia and then 1,3disubstituted-2,3-dihydro-1H-naphtoxazines were synthesized. The structures of the obtained new compounds have been clarified by spectroscopic methods and confirmed with elemental analysis results. From the synthesized compounds, 1,3-Di(2-naphthyl)-2,3-dihydro-1H-naphto[1,2-e][1,3]oxazine was investigation of the effects of solvent and concentration with UV-Visible Spectrophotometer. Additionally, this compound was analyzed the mutagenic and anti-mutagenic properties

2011-12-20T00:00:00Z