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세균의 활성산소종과 활성질소종에 대한 내성에서 NADH dehydrogenase-2 결손의 효과
박희정(Hee Jeong Park),채권석(Kwon Seok Chae),방일수(Iel Soo Bang) 대한구강악안면병리학회 2010 대한구강악안면병리학회지 Vol.34 No.6
The electron transport chain (ETC) delivers electrons from many substrates to reduce molecular oxygen to water. ETC accomplishes the stepwise transfer of electrons through series of protein complexes conferring oxidation-reduction reactions with concomitant transport of proton across membrane, generating a proton gradient which leads ATP synthesis by F0F1ATPase. Bacterial ETC initiates with oxidation of NADH by NADH dehydrogenase complex (complex Ⅰ). Therefore, damage of complex Ⅰ leads to insufficient function of ETC and accumulation of NADH inside the cell. Contribution of ETC activity and its consequent changes of NADH levels to bacterial damage response against reactive oxygen and nitrogen species (ROS/RNS) has been poorly understood. In this study, by constructing ndh mutant Salmonella lacking complex Ⅰ NADH dehydrogenase 2, we evaluated the effect of ETC deficiency to bacterial resistance against ROS and RNS. The growth of ndh mutant Salmonella is impaired in the culture media containing hydrogen peroxide, but rather accelerates in the media containing nitric oxide donors. Data suggest that redox potential of NADH accumulated inside the cell by ETC blockage may affect inversely to bacterial resistance against reactive oxygen species and reactive nitrogen species.
최정식,여성문,김웅석,채권석,Choi, Chung-Sik,Yoe, Sung-Moon,Kim, Eung-Seok,Chae, Kwon-Seok,Kim, Hak R. The Korean Society for Integrative Biology 1997 Korean journal of biological sciences Vol.1 No.3
Antibacterial activity was induced in the haemolymph of the common cutworm, Spodoptera litura by the artificial injection of E, coli Ek132. Antibacterial peptides were purified from the immunized haemolymph by heat treatment, ion-exchange chromatography, gel filtration chromatography, and reverse phase FPLC, and their physicochemical characteristics were investigated. These purified antibacterial peptides designated as spodopsin la and Ib were named after Spodoptera litura. Spodopsin la and Ib had the apparent molecular masses of 3, 823 Da and 3, 886 Da, respectively, and about 20% of the sequences had basic amino acids, such as lysine and arginine but no cysteine. Also, spodopsin l was confirmed to be a new member of cecropin family having a similar amino acid sequence to cecropin of lepidopteran insects, such as Bombyx mori and Hyalophora cecropia. The purified spodopsin was active against gram-positive as well as gram-negative bacteria.