A high-intensity LED LCU used for 10 seconds resulted in RH values greater than 80%, with all four restoratives tested indicating a sufficient degree of monomer conversion with such a short curing cycle.

This review describes the recent publications reported on the chemistry of 2-chloroquinoline-3-carbaldehydes. Heterocyclic quinoline ring systems are binary and fused cycles.

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The reaction of 5-amino-3-methylisoxazole with appropriate α,β-unsaturated ketones gave the corresponding isoxazolo[5,4-b]pyridines. Treatment of 1 with 2,6-dibenzylidenecyclohexanone or 2-benzylidenedimedone afforded the corresponding isoxazolo[5,4-b]quinoline derivatives. 4,6,8,9-Tetrahydroisoxazolo[5,4-b]quinolin-5-one derivative was also obtained by multicomponent condensation reaction of 1 with dimedone and benzaldehyde. Heterocyclic annulation of the isoxazolo[5,4-b]pyridine system was achieved via reaction of 1 with benzylidene derivatives of indandione, quinuclidone, pyrazolone, and oxazolone. A representative of some newly synthesized compounds was evaluated as antitumor agents.

Glucose-6-phosphate dehydrogenase from camel liver was purified to homogeneity by ammonium sulfate precipitation and a combination of DEAE-cellulose, Sephacryl S-300 gel filtration, and 2′, 5′ ADP Sepharose 4B affinity chromatography columns. The specific activity of camel liver G6PD is increased to 1.80438 units/mg proteins with 63-fold purification. It turned out to be homogenous on both native PAGE and 12% SDS PAGE, with a molecular weight of 64 kDa. The molecular weight of the native form of camel liver G6PD was determined to be 194 kDa by gel filtration indicating a trimeric protein. The K m value was found to be 0.081 mM of NADP+. Camel liver G6PD displayed its optimum activity at pH 7.8 with an isoelectric point (pI) of pH 6.6–6.8. The divalent cations MgCl2, MnCl2, and CoCl2 act as activators; on the other hand, CaCl2 and NiCl2 act as moderate inhibitors, while FeCl2, CuCl2, and ZnCl2 are potent inhibitors of camel liver G6PD activity. NADPH inhibited camel liver G6PD competitively with K i value of 0.035 mM. One binding site was deduced for NADPH on the enzyme molecule. This study presents a simple and reproducible purification procedure of G6PD from the camel liver.

A novel series of Schiff bases, hydrazide, and hydrazine derivatives containing quinoline moiety were synthesized via condensation of 3-substituted quinolines 1a and 1b with different aromatic amines or hydrazines. Furthermore, various heterocyclic ring systems: 1,3,4-thiadiazole, thiazolidin-4-one, 2-thioxoimidazolidin-4-one, and thiazole derivatives 10-13 were synthesized by refluxing hydrazinecarbothioamide derivative 9 with different acetic acid derivatives. Theoretical calculation of the title compounds were carried out using density functional theory method. The geometrical optimization of the prepared target compounds was theoretically analyzed. The synthesized compounds were examined for their antimicrobial and antioxidant activities. The obtained results revealed clearly that compounds 8 and 13 displayed promising activity as an antimicrobial activity and compounds 3, 5, 6, 7, and 9 exhibited better radical scavenging ability. Scheme 3. Transformation reaction of thiosemicarbazone derivative 9 to quinolone-attached 5-membered heterocyclic moieties 10-13. Scheme 2. Reaction of 2-substituted quinoline-3-carbaldehyde 1a and 1b with hydrazine derivatives.

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Blood-sucking arthropods have different types of anticoagulants to allow the ingestion of a blood meal from their hosts. In this study, five anticoagulants prolonging the activated partial thromboplastin time were resolved from the salivary gland crude extract of the camel tick Hyalomma dromedarii by chromatography on diethylaminoethyl (DEAE)-cellulose column. They were designated P1, P2, P3, P4 and P5 according to their elution order. P5 was found to be a potent thrombin inhibitor and purified by ultrafiltration through two centrifugal concentrators of 50 and 30 kDa molecular weight cut-off (MWCO), respectively. The camel tick salivary gland thrombin inhibitor was purified 60.6 folds with a specific activity of 564 units/mg protein. It turned out to be homogenous on native-PAGE with molecular weight of 36 kDa as detected on 12% SDS-PAGE. It inhibits bovine thrombin competitively with K value of 0.55 μM. A task for the future will be the elucidation of this thrombin inhibitor structure to allow its application in thrombosis treatment.