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KIM, JEONGEUN,KIM. SUKWHA,KIM, HEE-CHAN,KIM, KYUNG-HWAN,YANG, SEOK-CHUL,LEE, CHOON-TAEK,KONG, HYOUN-JOONG,LEE, KYUNGSOON Lippincott Williams Wilkins 2012 Computers, informatics, nursing Vol.30 No.12
<P> Through the use of ubiquitous health, or u-Health, services, medical information can be adapted and made accessible via computer and Internet to provide quality healthcare to anybody, any place, and any time. We developed and implemented u-Health services for patients with chronic obstructive pulmonary disease and studied their experiences with respect to their knowledge of chronic obstructive pulmonary disease and skill and attitude toward the u-Health devices. The u-Health services were composed of telemonitoring and teleconsultation supplemented with home visits. To determine its effectiveness, the u-Health service system was implemented for 2 years with 144 chronic obstructive pulmonary disease patients in a clinical experiment. The subjects were divided into three experimental groups, each provided with different services, compared before and after intervention, and among groups. The analysis of data gathered through the system suggested that u-Health services can support patients with chronic obstructive pulmonary disease, improve patients’ knowledge about chronic obstructive pulmonary disease self-management, build u-Health device usage skills, and foster a positive attitude toward u-Health devices. The u-Health services for the chronic obstructive pulmonary disease patients were both feasible and effective from the patients' perspective. </P>
Hyeon, Ji-Yeon,Hwang, Seoyeon,Kim, Hyejin,Song, Jaehyoung,Ahn, Jeongbae,Kang, Byunghak,Kim, Kisoon,Choi, Wooyoung,Chung, Jae Keun,Kim, Cheon-Hyun,Cho, Kyungsoon,Jee, Youngmee,Kim, Jonghyun,Kim, Kisang Centers for Disease Control and Prevention 2013 Emerging infectious diseases Vol.19 No.8
<P>The epidemiology of enteroviral infection in South Korea during 1999–2011 chronicles nationwide outbreaks and changing detection and subtyping methods used over the 13-year period. Of 14,657 patients whose samples were tested, 4,762 (32.5%) samples were positive for human enterovirus (human EV); as diagnostic methods improved, the rate of positive results increased. A seasonal trend of outbreaks was documented. Genotypes enterovirus 71, echovirus 30, coxsackievirus B5, enterovirus 6, and coxsackievirus B2 were the most common genotypes identified. Accurate test results correlated clinical syndromes to enterovirus genotypes: aseptic meningitis to echovirus 30, enterovirus 6, and coxsackievirus B5; hand, foot and mouth disease to coxsackievirus A16; and hand, foot and mouth disease with neurologic complications to enterovirus 71. There are currently no treatments specific to human EV infections; surveillance of enterovirus infections such as this study provides may assist with evaluating the need to research and develop treatments for infections caused by virulent human EV genotypes.</P>
Responses of spinal dorsal horn neurons to foot movements in rats with a sprained ankle.
Kim, Jae Hyo,Kim, Hee Young,Chung, Kyungsoon,Chung, Jin Mo American Physiological Society [etc.] 2011 Journal of neurophysiology Vol.105 No.5
<P>Acute ankle injuries are common problems and often lead to persistent pain. To investigate the underlying mechanism of ankle sprain pain, the response properties of spinal dorsal horn neurons were examined after ankle sprain. Acute ankle sprain was induced manually by overextending the ankle of a rat hindlimb in a direction of plantarflexion and inversion. The weight-bearing ratio (WBR) of the affected foot was used as an indicator of pain. Single unit activities of dorsal horn neurons in response to plantarflexion and inversion of the foot or ankle compression were recorded from the medial part of the deep dorsal horn, laminae IV-VI, in normal and ankle-sprained rats. One day after ankle sprain, rats showed significantly reduced WBRs on the affected foot, and this reduction was partially restored by systemic morphine. The majority of deep dorsal horn neurons responded to a single ankle stimulus modality. After ankle sprain, the mean evoked response rates were significantly increased, and afterdischarges were developed in recorded dorsal horn neurons. The ankle sprain-induced enhanced evoked responses were significantly reduced by morphine, which was reversed by naltrexone. The data indicate that movement-specific dorsal horn neuron responses were enhanced after ankle sprain in a morphine-dependent manner, thus suggesting that hyperactivity of dorsal horn neurons is an underlying mechanism of pain after ankle sprain.</P>
Reduction of Nitrosoarene by Purified NAD(P)H-Quinone Oxidoreductase
Kim, KyungSoon,Suk, Heewon The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.4
NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified from S. cerevisiae. The enzyme readily reduced 2,6-dichlorophenolindophenol, a quinonoid redox dye, as well as substituted benzo- and naphthoquinones, and could accept electrons from either NADH or NADPH. The purified NAD(P)H-quinone oxidoreductase turned out to be capable of reducing nitrosoarenes as well as a variety of quinones. A chemical-trapping technique using 4-chloro-1-naphthol was used to show that the N,N-dimethyl-p-benzoquinonediiminium cation was produced in the reduction of 4-nitroso-N,N-dimethylaniline catalyzed by NAD(P)H-quinone oxidoreductase.
Reduction of Azobenzene by Purified Bovine Liver Quinone Reductase
Kim, Kyungsoon,Shin, Hae-Yong The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.4
Quinone reductase was purified to homogeneity from bovine liver by using ammonium sulfate fractionation, ion-exchange chromatography, and gel filtration chromatography. The enzyme utilized either NADH or NADPH as the electron donor. The enzyme catalyzed the reduction of several quinones and other artificial electron acceptors. Furthermore, the enzyme catalyzed NAD(P)H-dependent reduction of azobenzene. THe apparent Km for 1,4-bezoquinone and azobenzene was 1.64mM and 0.524mM, respectively. The reduction of azobenzene by quinone reductase was almost entirely inhibited by dicumarol or Cibacron blue 3GA, potent inhibitors of the mammalian quinone reductase. In the presence of 1.0μM Cibacron blue 3GA, azoreductase activity was lowered by 45%, and almost complete inhibition was seen above 2.0μM Cibacron blue 3GA.
Biochemical Properties NAD(P)H-Quinone Oxidoreductase from Saccharomyces cerevisiae
Kim, Kyungsoon,Suk, Heewon The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.2
The NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified from S. cerevisiae. The native molecular weight of the enzyme is approximately 111 kDa and is composed of five identical subunits with molecular weights of 22 kDa each. The optimum pH of the enzyme is pH 6.0 with 1,4-benzoquinone as a substrate. The apparent K m for 1,4-benzoquinone and 1,4-naphthoquinone are 1.3 mM and 14.3 μM, respectively. Its activity is greatly inhibited by Cu²+ and Hg²+ ions, nitrofurantion dicumarol, and Cibacron blue 3GA. The purified NAD(P)H-quinone oxidoreductase was found capable of reducing aromatic nitroso compounds as well as a variety of quinones, and can utilize either NADH or NADPH as a source of reducing equivalents. The nitroso reductase activity of the purified NAD(P)H-quinone oxidoreductase is strongly inhibited by dicumarol.
Characterization of 1,4-Benzoquinone Reductase from Bovine Liver
Kim, Kyungsoon The Korean Society for Biotechnology and Bioengine 2002 Biotechnology and Bioprocess Engineering Vol.7 No.4
1,4-Benzoquinone reductase was purified to electrophoretic homogeneity from bovine liver, and the purified enzyme found to have a molecular mass of 29 kDa, as determined by sodium dodecyl sulfate- polyacrylamide gel electrophoresis The enzyme exhibited pH optimum between 8.0 and 8.5. The apparent fm for 1,4-benzoqulnone was 1.643 mM, and the apparent Km for NADH was 1.837 mM. Various divalent cations, such as Hg$\^$2+/, Cu$\^$2+/, and Zn$\^$2+/, exhibited strong inhibitory effects. The enzyme activity was also strongly inhibited by quercetin, dicumarol, and benzoic acid. Incubation of the enzyme with N-bromosuccinimide and pyridoxal 5’-phosphate led to inhibitions of 100% and 99%, respectively. Accordingly, these results suggest that trypto-phan and Iysine residues are Involved at or near the active sites of the enzyme.