Emittance Growth Caused by Current Variation in a Beam-Transport Channel
Time variation of space-charge forces in a beam-transport channel will lead to a time-averaged emittance growth of the beam. The Kapchinskii-Vladimirskii (K-V) equations have been used to follow the envelope of a round beam with effective beam current fluctuation i through a transport channel. The area of the ellipse that encloses the varying ellipses at the end has been used as the criterion for emittance growth. Simple formulae give the relation between i, initial emittance ¿, allowable fractional emittance growth ¿¿, effective average current I, average beam radius R, and transport length. For example, for a long transport channel a nominally compensated beam must have i <(ß¿¿2I0/R2)¿¿, where I0 = 4¿¿0Mc3/e, and ß¿ is the usual relativistic factor. Results for other conditions are presented. A comparison with a numerical calculation from the TRACE code for transport of a 100-keV, 100-mA beam is made.
The 4X Source
Our Penning surface-plasma source (SPS) discharge chamber was enlarged 4X in two dimensions. To date, three pulsed discharge modes have been studied: two with noisy arc (¿20% H- current fluctuations) and one with quiescent arc (¿1% H- current fluctuations). Lower arc magnetic field and higher H2 gas flow allow switching from the noisy to the quiescent mode. The noisy modes yield up to 120 mA of 29-keV H- beam; for 110 mA at 29 keV, the two-dimensional normalized rms emittance is 0.017 x 0.018 ¿·cm·mrad. The quiescent mode yields 75 mA of 29-keV H- beam; for 67 mA at 24 keV, the emittance is 0.011 x 0.012 ¿·cm·mrad.
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.