Novel transformer active filters
Novel transformer active filters are proposed to obtain high attenuation of voltage or current ripple without deteriorating the transient response of the system considered. Experimental results show that the scheme gives good steady-state performance of the power supply. >
Novel load ripple voltage-controlled parallel DC active power filters for high performance magnet power supplies
The cooling storage ring of the heavy ion research facility in Lanzhou (HIRFL-CSR) is one of the five mega-science projects undertaken by Chinese Academy of Science within its ninth and tenth five-year plan period. The HIRFL-CSR facility can providing heavy ion beams in wide energy range, manifold and with high quality. This paper presents a hybrid filter structure consisting of a passive filter and a parallel dc active power filter (DCAPF) for a sample magnet power supply in HIRFL-CSR. The configuration of the power system with the DCAPF is introduced. Then a novel feedback control scheme for the DCAPF is proposed with detecting the output ripple voltage across the magnet load. For detailed discussion, a simple model of the whole system has been derived and the stability characteristic is analyzed. Through simulation and experiment investigation, the DCAPF is successfully applied in a 120-kW magnet power supply in HIRFL-CSR finally. The ripple factor and tracking accuracy of the output current through the load achieve 8.87 ppm and 100 ppm, respectively. Therefore, the rigor requirements of low output current ripple and fast ramp rate are both satisfied with the DCAPF proposed.
Chemical, biological, and immunological characterization of mono- and diiodothyrotropin releasing factor.
Abstract Iodination of thyrotropin releasing factor (TRF) with chloramine-T and NaI at pH 7.5 produces both mono- and diiodo-TRF as well as unreacted TRF and I − . The four compounds can be separated by ion-exchange chromatography on SP-Sephadex C-25, using a stepwise gradient of 0.01 m MH 4 OAc at pH 3.5, 5.2 and 7.2. The monoiodo-TRF was characterized by nuclear magnetic resonance, mass spectra, and elemental analysis as [Im-5-iodo-His 2 ]-TRF while the diiodo-TRF was similarly characterized as [Im-2,5-diiodo-His 2 ]-TRF. Both iodination products showed no thyrotropin releasing activity at doses up to 1 μg in the in vivo mouse bioassay. The specific binding of mono- and diiodo-TRF was measured against three different TRF antisera. In the absence of TRF, antisera A and C bound more diiodo-TRF than monoiodo-TRF while antiserum B seemed to bind both tracers equally. In all cases steeper curves were produced when diiodo-TRF was displaced by synthetic TRF.