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Evaluation on Insulation Performance of Traction Motors for a Hybrid Vehicle by Partial Discharge Measurement (부분방전 측정에 의한 하이브리드차량 견인전동기의 절연성능평가)

  • Park, Dae-Won;Park, Chan-Yong;Choi, Jae-Sung;Kil, Gyung-Suk;Lee, Kang-Won
    • Journal of the Korean Society for Railway
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    • v.12 no.2
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    • pp.249-253
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    • 2009
  • This paper dealt with the insulation evaluation by a measurement of partial discharge(PD) on traction motors used in a hybrid vehicle. The PD method has been accepted as an effective and a non-destructive. technique to evaluate insulation performance of low-voltage electric and electronic devices. In this paper, the PD measurement system which was manufactured with a coupling network, a low noise amplifier, and an associated electronics is described. The PD measurement system has the frequency bandwidth of $1[MHz]{\sim}30[MHz]$ at -3 [dB] and the stable sensitivity of 19 [mV/pC] for the traction motor. From the experimental results, discharge inception voltage (DIV) and apparent charge (q) were $1,100[V_{rms}]$ and 105 [pC] for the used motor, and $1,400[V_{rms}]$ and 84 [pC] for the new one. By comparing the DIV and q, we could evaluate the insulation condition for the traction motors.

Synthesis of Resin Derivatives and Purification of Protein - Synthesis of p-Aminoanilinylsuccinyl-AH-Sepharose 4B and Purification of Protein in Pleurotus cornucopiae - (친화성 고분자 유도체의 합성 및 단백질의 분리정제에 관한 연구 - p-Aminoanilinylsuccinyl-AH-Sepharose 4B의 합성 및 흰느타리버섯 중 단백질의 정제 -)

  • Min, Tae-Jin;Kim, Yong-Rip;Park, Sang-Shin;Lee, Soo-Yong
    • The Korean Journal of Mycology
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    • v.17 no.3
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    • pp.105-113
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    • 1989
  • For selective purification of proteins in Pleurotus cornucopiae, affinity chromatography was performed by p-aminoanilinylsuccinyl-AH-Sepharose 4B gel synthesized by treating p-phenylene diamine with succinyl-AH-Sepharose 4B, which was prepared by treating AH-Sepharose 4B with succinic anhydride. The capacity of p-aminoanilinyl ligand group was 6.1 micromole per milliliter of gel. Total apparent molecular weight of the affinity proteins eluted from the synthesized gel was 167 KD, which were a protein complex of 130 KD and 37 KD. The contents of the nonpolar, polar, positively and/or negatively charged amino acids in the affinity protein were 44.57%, 24.75%, 21.25%, and 9.43%, respectively. Total apparent molecular weight of the affinity proteins eluted from the AH-Sepharose 4B gel was 95.2 KD, which were a protein complex of 61 KD, 31 KD and 3.2 KD. The contents of the nonpolar, positively and/or negatively charged amino acids in the affinity protein by AH-Sepharose 4B gel were 44.05%, 29.13%, and 12.91% respectively.

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