Activation Process of Impregnated Dispenser Cathode Viewed in the Large-screen Emission Microscope†

1962 ◽  
Vol 13 (5) ◽  
pp. 401-416 ◽  
Author(s):  
AURELIUS SANDOR
Author(s):  
Nergis Yildiz Angin Atmaca ◽  
Emirhan Postaci ◽  
Hasan Erciyas ◽  
Ozlem Akman Gokcel ◽  
Selahattin Nesil ◽  
...  

Author(s):  
T. Koshikawa ◽  
Y. Fujii ◽  
E. Sugata ◽  
F. Kanematsu

The Cu-Be alloys are widely used as the electron multiplier dynodes after the adequate activation process. But the structures and compositions of the elements on the activated surfaces were not studied clearly. The Cu-Be alloys are heated in the oxygen atmosphere in the usual activation techniques. The activation conditions, e.g. temperature and O2 pressure, affect strongly the secondary electron yield and life time of dynodes.In the present paper, the activated Cu-Be dynode surfaces at each condition are investigated with Scanning Auger Microanalyzer (SAM) (primary beam diameter: 3μmϕ) and SEM. The commercial Cu-Be(2%) alloys were polished with Cr2O3 powder, rinsed in the distilled water and set in the vacuum furnance.Two typical activation condition, i.e. activation temperature 730°C and 810°C in 5x10-3 Torr O2 pressure were chosen since the formation mechanism of the BeO film on the Cu-Be alloys was guessed to be very different at each temperature from the results of the secondary electron emission measurements.


1978 ◽  
Vol 40 (02) ◽  
pp. 350-357
Author(s):  
Robert H Yue ◽  
Menard M Gertler

SummaryThe binding of Ca+2 to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of 45Ca+2. The binding data are consistent with a model of sequential mechanism. One mole of Ca+2 binds to the glycoprotein with a dissociation constant of 5.2 × 10-5 M and an additional 39 ± 4 moles of Ca+2 bind to this zymogen with a dissociation constant of 3.7 × 10-3M. The binding of the high affinity Ca+2 causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell’s viper venom.


2016 ◽  
Vol 2016 (1) ◽  
pp. 142-146 ◽  
Author(s):  
Taeseong Han ◽  
Sungjin Kim ◽  
Dongwoo Kang
Keyword(s):  

2012 ◽  
Vol 52 (4) ◽  
pp. 421-432 ◽  
Author(s):  
Michael D. McNiven ◽  
Dean Krugman ◽  
Spencer F. Tinkham

2012 ◽  
Vol 27 (5) ◽  
pp. 480-484 ◽  
Author(s):  
Yun-Tao CUI ◽  
Jin-Shu WANG ◽  
Wei LIU ◽  
Xi WANG ◽  
Kai-Feng WANG

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