• Title/Summary/Keyword: 한복관여

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The Influence of Consumer's Involvement and Arousal Seeking Tendency on Preference of Hanbok and Purchasing Behavior of Hanbok (소비자의 관여와 감각추구성향이 한복선호도와 한복구매행동에 미치는 영향)

  • Kim, Soon Ah
    • Journal of the Korean Society of Clothing and Textiles
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    • v.46 no.2
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    • pp.349-366
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    • 2022
  • The purpose of this study was to reveal the influence of consumers' Hanbok involvement and arousal seeking tendency on their Hanbok preference and purchasing behavior. The survey subjects were male and female consumers ranging in age from teens to those in their fifties. An online survey was conducted, and 627 people were analyzed. Version 26.0 of SPSS was used to perform a t-test as well as frequency, correlation, factor, reliability, and regression analyses. As a result, both Hanbok involvement and arousal seeking tendency derived four factors each. All four factors of Hanbok involvement had a significant effect on Hanbok preference. Two factors of arousal seeking tendency had a significant effect on Hanbok preference. Hanbok preference had a partially significant effect on Hanbok purchasing behavior. Hanbok involvement and arousal seeking tendency had a partially significant impact on Hanbok purchasing behavior. In conclusion, this study is meaningful in that it, for the first time, derived the factor of Hanbok involvement by considering the concept of involvement as it relates to Hanbok and identified that involvement and arousal seeking tendency are variables that affect Hanbok preference and purchasing behavior.

Isolation of Lactobacillus plantarum HB1 from Tongchimi and Its Nitrite-Scavenging Effect (동치미로부터 분리된 유산균 Lactobacillus plantarum HB1의 아질산염 소거 효과)

  • 유형재;이선숙;이동석;김한복
    • Korean Journal of Microbiology
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    • v.39 no.3
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    • pp.192-196
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    • 2003
  • To obtain large pools of lactic acid bacteria, a strain was isolated from Tongchimi. Through its sugar fermentation and analysis of 16S rRNA gene, it was identified to be Lactobacillus plantarum HB1. This strain is Gram-positive and catalase-negative. In the range of 1~88 bp in the HB1 16S rRNA gene, the HB1 strain was homologous with other L. plantarum strains by almost 100%, and in the range of the rest 32 bp, the HB1 strain showed considerable variation, compared to other strains. Nitrate which may exist in radish can be easily converted to nitrite. The nitrite interacts with amine, and becomes nitrosamine which may cause stomach cancer. The culture obtained by HB1 strain could eliminate 400 ${\mu}M$ nitrite within 1.5 hr. It is necessary to isolate specific components which are involved in nitrite elimination in the culture and to study on its mechanism.

The Effect of Vanadate on the Optimum pH of Na-K-ATPase and $K^+-pNPPase$ in Rabbit Kidney Cortex (가토 신장 Na-K-ATPase 및 $K^+-pNPPase$의 최적 PH에 미치는 Vanadate의 영향)

  • Ea, Yun-Sun;Woo, Jae-Suk;Han, Bok-Ki;Lee, Sang-Ho
    • The Korean Journal of Physiology
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    • v.18 no.2
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    • pp.163-169
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    • 1984
  • The effect of vanadate on the optimum pH of Na-K-ATPase was investigated. The results were as follows: 1) The optimum PH of Na-K-ATPase was shifted from PH 7.4 to 6.8 at 10 mM K by $5{\times}10^{-6}M$ vanadate. 2) The ratio of Na-K-ATPase activity at pH 6.8 and 7.4 increased with increasing vanadate concentration. 3) Inspite of the presence of $5{\times}10^{-6}M$ vanadate Na-K-ATPase activity at pH 7.4 was higher than that at pH 6.8 below 50 mM $Na^+$, and the ratio of Na-K-ATPase activity at pH 7,4 and 6.8 was higher than that of the control. 4) Na-K-ATPase activity at pH 7.4 was higher than that at pH 6.8 below 7mM $K^+$. 5) Optimum pH of Na-K-ATPase activity was shifted from pH 7.4 to 6.8 by $10^{-5}M$ vanadate at 5 mM $K^+$. 6) $K^+$-pNPPase activity increased with lowering of pH, and the degree of inhibition of $K^+$-pNPPase activity by $10^{-7}$M vanadate was decreased with lowering of pH. These results suggest that vanadate shifts the optimum pH of Na-K-ATPase activity to more acidic PH than PH 7.4. This effect may not be caused by the decrease in the inhibitory potency of vanadate itself to Na-K-ATPase by the change of medium pH, but mainly by the alteration of Na-and K-binding site, which appears in the presence of vanadate only.

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