Search

A new isotope 203Ac was produced in the reaction 40Ca + 169Tm at beam energy of 226 MeV. One correlated α-decay chain was attributed to 203Ac. The α-particle energy and half-life were determined to be 8217(16) keV and 56−26+269 μs, respectively. The reduced α-decay width (δ2) of 203Ac was deduced to be 1096−906+921 keV, which indicates a favored α decay. The systematics of δ2 and single-particle energy levels indicate that the new state probably arises from the intruder s1/2 configuration, which shows an onset of deformation in Ac isotopes. The proton separation energy Sp of 203Ac was extracted as −1214(22) keV and the systematics of Sp for odd-A isotopes beyond proton drip line were discussed.

A new proton-unbound isotope 204Ac was produced in the fusion-evaporation reaction Tm(40169Ca,5n)204Ac and identified via the recoil-α correlation at the gas-filled recoiled separators SHANS2 and SHANS. The excitation function for producing 204Ac was measured and the optimal beam energy was evaluated to be 212 MeV. Nineteen ER - α1 - α2 - α3 decay chains were observed for this isotope. Based on these chains, the α-particle energy and half-life of 204Ac were determined to be 7948(15) keV and 7.4−1.4+2.2 ms, respectively. Both are consistent with the theoretical prediction. The reduced α-decay width was deduced to be 49−15+10 keV, which indicates a favored α decay for 204Ac. In addition, more precise decay properties of Eα = 7883(15) keV and T1/2 = 7.7−1.6+2.7 ms were obtained for 205Ac.

This paper describes scalings of the H-mode confinement database of neutral beam injection (NBI)-lower hybrid wave (LHW) and electron cyclotron resonant heating-LHW plasmas in the EAST tokamak. Fundamental information of the EAST H-mode database and the details of calculation of the thermal energy confinement time in EAST are presented. The result of the scaling model ${\tau _{{\text{E,EASTS,H,NBI - LHW}}}}$ of the thermal energy confinement time in NBI-LHW plasmas with root-mean-square-error ${\text{RMSE}} = 5.5\% $ , compared with the multi-machine scaling model ${\tau _{{\text{th,98}}y{\text{2}}}}$ derived from the multi-machine database (mainly NBI heating) with ${\text{RMSE}} = 12.9\% $ , is obtained. The scaling ${\tau _{{\text{E,EAST,H,NBI - LHW}}}}$ presents a similar dependency on plasma current and power loss and a lower dependency on plasma density and elongation, but stronger dependency on toroidal field than in ${\tau _{{\text{th,98}}y{\text{2}}}}$ . The scaling ${\tau _{{\text{E,EAST,H,ECRH - LHW}}}}$ demonstrates a similar dependency on plasma current and power loss and lower dependency on plasma density, but a negative dependency with large error bars on elongation compared with ${\tau _{{\text{E,EAST,H,NBI - LHW}}}}$ in NBI-LHW plasmas. The comparison of EAST models with the more recent multi-tokamak scaling ITPA20-IL shows a similar engineering dependency on plasma current, power loss and plasma density, but opposite dependency on toroidal field.

A simple phase-transfer protocol that can uniquely identify core-shell Ag-Pt nanoparticles prepared by the seed-mediated growth method is presented. It was found that core-shell Ag-Pt nanoparticles could be obtained by the seed-mediated growth method using Ag nanoparticles as the seeds.

In order to investigate the protective effect of outer membrane protein A (OmpA) against Enterobacteriaceae infection in mice, ompA gene was cloned from bovine mastitis E. coli 308-2 isolate, and then the recombinant OmpA protein was expressed and purified. SDS-PAGE detected recombinant OmpA protein and Western blotting confirmed that the protein had an average molecular weight of 60 kDa. Immunological analysis indicated that OmpA protein induced high level of antibodies, IFN-γ and IL-4 cytokines. Moreover, OmpA protein not only conferred a high level of immunogenicity to protect the immunized mice against the challenge of E. coli, but also generated protection against Klebsiella pneumonia and Shigella flexneri. From the data generated during the study it was suggested that OmpA could be selected as a potential candidate for vaccine against Enterobacteriaceae. [ABSTRACT FROM AUTHOR]