Deoxygenation of glycerol in aqueous medium catalyzed by Pt/WO 3 /ZrO 2 at relatively low temperatures (110-140 • C) under hydrogen pressure range from 2 to 5 MPa in a fixed-bed continuous-flow reactor gives 1,3-propanediol (1,3-PDO) and n-propanol (n-PrOH) as the predominant products, indicating high selectivity for deoxygenation of the secondary hydroxyl group over the primary hydroxyl groups of the glycerol. The optimum catalyst was prepared by calcination of WO 3 /ZrO 2 at 700 • C and loading of 3.0 wt% Pt with W content of 10 wt%. The effect of reaction temperature, hydrogen pressure and initial water content were evaluated to find the optimum reaction conditions. The glycerol conversion and the yield of 1,3-PDO greatly depended on these factors. At 130 • C, 4 MPa and 70.2% conversion, the yield of 1,3-PDO was up to 32.0% (1,3-PDO/1,2-PDO = 17.7). The proposed mechanism for glycerol deoxygenation in aqueous medium over Pt/WO 3 /ZrO 2 is an ionic pathway involving proton and hydride ion transfer steps.

Electrical stimulation is safe during IONM in this porcine model. Minimal current that required generating the maximal evoked EMG, approximately 1 mA in this study, can be selected to minimize the risk of nerve damage and cardiopulmonary effects.

Ethylene (C2H4) purification from multicomponent mixtures by physical adsorption presents a great challenge in the chemical industry. This work successfully uses the postsynthetic method of crystal transformation in boiling alkaline solution to synthesize a trap‐and‐flow channel crystal (namely NTU‐67), the flow channel of which provides an effective shape‐ and size‐dependent sieving path for linear molecules such as acetylene (C2H2) and carbon dioxide (CO2), while the adjacent channel possesses customized space for efficient molecular trapping. The three‐bladed array of the nanospace enables the crystal to afford a record productivity of C2H4 (121.5 mL g−1, >99.95%) from C2H2/CO2/C2H4 (1/9/90, v/v/v) mixtures in a single adsorption–desorption cycle under humid and dynamic conditions, even at a high temperature of 343 K and wide gas ratio. The molecular‐level insight and mechanism of the cooperative role of the trap‐and‐flow channel, found computationally and observed experimentally, demonstrates a new design philosophy toward extending the application boundaries of porous coordination polymers to further challenging tasks.

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Three agglutinins (lectins), designated BDL1, BDL2 and BDL3, were identified in the haemolymph of the cockroach Blaberus discoidalis by erythrocyte cross-adsorption and sugar inhibition tests. With the use of (NH4)2SO4 fractionation, anion-exchange and affinity chromatography, BDL1 and BDL2 have been purified to homogeneity, and BDL3 has been partially purified to three bands on SDS/PAGE. BDL1 has a molecular-mass estimate of 390 kDa by gel filtration and approx. 158 kDa by SDS/PAGE under non-reducing conditions, further reduced to subunits of 36 kDa under reducing conditions. BDL2 has a molecular mass of approx. 140 kDa and is composed of subunits of 67 kDa which can be further reduced to identical subunits of 23 kDa. Isoelectric focusing in agarose gels revealed that BDL1 and BDL2 both focused as single bands at pH 6.0 and pH 5.2 respectively. The purified forms of BDL1 and BDL2 were stained by the periodic acid/Schiff's reagent showing that both lectins are glycoproteins. In addition, BDL1 was deglycosylated by endo-beta-N-acetylglucosaminidase H. Immunological tests showed that these three lectins are not structurally related. All three lectins bind galactose but have different specificities for binding other sugars and for a range of vertebrate erythrocytes. BDL1 is specifically inhibited by D-(+)-glucose, D-(+)-mannose and N-acetyl-D-mannosamine, but not by N-acetyl-D-glucosamine, and BDL2 is inhibited by N-acetyl-D-glucosamine, but not by D-(+)-glucose, D-(+)-mannose or N-acetyl-D-mannosamine. BDL3 is strongly inhibited by N-acetyl-D-galactosamine, but not by any of the other above-mentioned sugars. Erythrocyte specificities showed that BDL1 is more specific for rabbit than mouse erythrocytes, whereas BDL2 and BDL3 are more specific for mouse than rabbit erythrocytes. The haemagglutinating activities of both the serum and isolated lectins are Ca(2+)-dependent. Localization of BDL1 and BDL2 with fluorescein isothiocyanate-labelled antibodies showed that both lectins are associated with the granules and other areas of the cytoplasm of all blood cell types.

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