• Title/Summary/Keyword: Hack to Hog

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Development of Shot Accuracy Trainer for Wheelchair Curling (휠체어 컬링 샷 정확도 향상을 위한 훈련장비 개발)

  • Kil, Se Kee;Lee, Hyun Been;Kim, Tae Whan;Lee, Sang Cheol;Hwang, Jong Hak;Shim, Hyun Min;Han, Young Hwan
    • Journal of rehabilitation welfare engineering & assistive technology
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    • v.11 no.4
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    • pp.377-383
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    • 2017
  • In this study, it is proposed and developed a shot accuracy trainer for wheelchair curling. This trainer is developed to improve curling shot accuracy by supplying functions of changing guide width in which curling stone passes by and of time mesurement of Hack to Hog. And it also can supply training video of athlete to coach to analyze. From the pilot test from coaching staff of wheelchair curling team, association executives and icemaker of rink, we tried to verify the usability of proposed system.

des-$Asp^4$-Amastatin, MRK-22 as an Inhibitor of Aminopeptidase M produced by Streptomyces sp. SL20209

  • Kho, Yung-Hee;Ko, Hack-Ryong;Chun, Hyo-Kon;Kim, Seung-Ho;Sung, Nack-Kie
    • Journal of Microbiology and Biotechnology
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    • v.5 no.3
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    • pp.154-157
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    • 1995
  • MRK-22, an inhibitor of aminopeptidase M was isolated from the culture broth of Streptomyces sp. SL20209. The structure of MRK-22 was defined to be 3-amino-2-hydroxy-5-methylhexanoyl-valyl-valine, des-$Asp^4$-amastatin, by spectroscopic analysis and this was also confirmed by solid phase synthesis of the inhibitor. The molecular formula and weight of MRK-22 were $C_17H_33N_3O_5$ and MW 359($M^+$), respectively, and its $IC_50$ value against hog kidney AP-M was 0.79 $\mu$ g/ml.

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Valistatin (3-Amino-2-Hydroxy-4-Phenylbutanoyl-Valyl-Valine), a New Aminopeptidase M Inhibitor, Produced by Streptomyces sp. SL20209

  • Kho, Ying-Hee;Ko, Hack-Ryong;Chun, Hyo-Kon;Jung, Myung-Chul
    • Journal of Microbiology and Biotechnology
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    • v.5 no.1
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    • pp.36-40
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    • 1995
  • Valistatin, a new inhibitor of aminopeptidase M(AP-M) was discovered in the culture broth of Streptomyces sp. SL20209 isolated from a soil sample. The inhibitor was purified by extraction with n-butanol and the various column chromatographies, and then isolated as whitish powder. The $^1 H-and ^1 H, ^1 H-COSY$ NMR studies, amino acid analysis, and fragmentation patterns by FAB-MS suggested the presence of one 3-amino-2-hydroxy-4-phenylbutanoic acid and two valine residues in the inhibitor. Thus, the structure of valistatin was determined as 3-amino-2-hydroxy-4-phenylbutanoyl-valyl-valine. Valistatin has the molecular formular $C_20H_31N_3 O_5$ (MW 394), and its $IC_50$ value against hog kidney AP-M was determined to be 3.12 $mu g/ml$.

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