http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
A Hybrid Algorithm Using Shape and Topology Optimization for the Design of Electric Machines
Jung, Seok-Won,Ro, Jong-Suk,Jung, Hyun-Kyo IEEE 2018 IEEE transactions on magnetics Vol.54 No.3
<P>The conventional topology optimization (TO) algorithm for an electric machine has a critical problem as the derivation of the impractical model to manufacture. In the case of a conventional step optimization, such as shape optimization (SO) after TO, the optimized model by TO is seriously distorted. To solve these problems, a hybrid optimization algorithm that conducts SO and TO simultaneously with the pre-processing and the post-processing is proposed in this paper.</P>
Jung, Won-Kyo,Jo, Hee-Yeon,Qian, Zhong-Ji,Jeong, Young-Ju,Park, Sae-Gwang,Choi, Il-Whan,Kim, Se-Kwon Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.5
A novel inhibitory protein against blood coagulation factor Va (FVa) was purified from muscle protein of granulated ark (Tegillarca granosa, order Arcoida, marine bivalvia) by consecutive FPLC method using anion exchange and gel permeation chromatography. In the results of ESI-QTOF tandem mass analysis and database research, it was revealed that the purified T. granosa anticoagulant protein (TGAP) has 7.7 kDa of molecular mass and its partial sequence, HTHLQRAPHPNALGYHGK, has a high identity (64%) with serine/threonine kinase derived from Rhodopirellula baltica (order Planctomycetales, marine bacteria). TGAP could potently prolong thrombin time (TT), corresponding to inhibition of thrombin (FIIa) formation. Specific factor inhibitory assay showed that TGAP inhibits FVa among the major components of prothrombinase complex. In vitro assay for direct-binding affinity using surface plasmon resonance (SPR) spectrometer indicated that TGAP could be directly bound with FVa. In addition, the binding affinity of FVa to FII was decreased by addition of TGAP in dose-dependant manner ($IC_{50}$ value = 77.9 nM). These results illustrated that TGAP might interact with a heavy chain of FVa ($FVa_H$) bound to FII in prothrombin complex. The present study elucidated that non-cytotoxic T. granosa anticoagulant protein (TGAP) bound to FVa can prolong blood coagulation time by inhibiting conversion of FII to FIIa in blood coagulation cascade. In addition, TGAP did not significantly (P < 0.05) show fibrinolytic activity and cytotoxicity on venous endothelial cell line (ECV 304).