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Magnetization of the stack of HTS tapes
Osipov, M.A.,Abin, D.A.,Pokrovskiy, S.V.,Mineev, N.A.,Rudnev, I.A. The Korea Institute of Applied Superconductivity a 2015 한국초전도저온공학회논문지 Vol.17 No.1
New results of dependence of magnetic field, trapped by a stack of HTS tapes, on amount of tapes in a stack are reported. Commercial GdBCO tape 12 mm width and without Cu layer was used for the research. Tape was divided in square pieces $12{\times}12mm^2$ from which stacks were formed. Filling factor of the tape was about 1.4%. Measurements were carried out for stacks with height from 5 to 250 pieces and at wide temperature range from liquid helium to liquid nitrogen. Both FC (field cooling) and ZFC (zero field cooling) cooling methods were used in the research. These two methods show matching results with good accuracy. As a result dependences of trapped magnetic flux on amount of tapes for different temperatures were received. Research shows, that with increasing height of the stack trapped magnetic field value reach saturation at about 60 tapes in a stack for low temperatures. From 60 to 100 tapes increase of magnet flux is only 5%. Thus increase amount of tapes in a stack is not profitable. Also investigation of trapped magnet field relaxation was carried out. Relaxation speed decreases with increasing amount of elements. It means that the higher the stack is, the longer trapped flux will be held in cause of the same temperature.
A study of ribonuclease activity in venom of vietnam cobra
( Thiet Van Nguyen ),( A. V. Osipov ) 한국축산학회(구 한국동물자원과학회) 2017 한국축산학회지 Vol.59 No.9
Background: Ribonuclease (RNase) is one of the few toxic proteins that are present constantly in snake venoms of all types. However, to date this RNase is still poorly studied in comparison not only with other toxic proteins of snake venom, but also with the enzymes of RNase group. The objective of this paper was to investigate some properties of RNase from venom of Vietnam cobra Naja atra. Methods: Kinetic methods and gel filtration chromatography were used to investigate RNase from venom of Vietnam cobra. Results: RNase from venom of Vietnam cobra Naja atra has some characteristic properties. This RNase is a thermostable enzyme and has high conformational stability. This is the only acidic enzyme of the RNase A superfamily exhibiting a high catalytic activity in the pH range of 1-4, with pH<sub>opt</sub> = 2.58 ± 0.35. Its activity is considerably reduced with increasing ionic strength of reaction mixture. Venom proteins are separated by gel filtration into four peaks with ribonucleolytic activity, which is abnormally distributed among the isoforms: only a small part of the RNase activity is present in fractions of proteins with molecular weights of 12-15 kDa and more than 30 kDa, but most of the enzyme activity is detected in fractions of polypeptides, having molecular weights of less than 9 kDa, that is unexpected. Conclusions: RNase from the venom of Vietnam cobra is a unique member of RNase A superfamily according to its acidic optimum pH (pH<sub>opt</sub> = 2.58 ± 0.35) and extremely low molecular weights of its major isoforms (approximately 8.95 kDa for RNase III and 5.93 kDa for RNase IV).