• Journal of Plant Biology
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• v.35 no.2
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• pp.117-123
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• 1992

The effect of benzyladenine (BA) on lipid peroxidation and compositions of total insoluble proteins and chloroplast thylakoid protein from wheat primary leaves during senescence in the dark was studied. BA ($10^{-5}\;M$) treatment prevented conspicuously the loss of chlorophyll content and soluble and insoluble leaf protein contents in senescing wheat leaf segments during 4-day dark incubation. Under the BA treatment, especially, the level of insoluble protein was highly maintained than that of soluble protein. Also, the increase of malondialdehyde (MDA: the peroxidation product of membrane lipids) content was inhibited in the BA treated leaves. Three major polypeptide bands in quantity corresponding to 57, 26 and 12 KD molecular weight were clearly resolved with other minor bands by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) in the insoluble protein fraction. The insoluble protein profiles of the control leaves showed a remarkable decrease in the intensity of the 57 and 12 KD band except for 26 KD band in the 72 h dark incubation. This loss during dark incubation was reduced by BA treatment. More than 20 polypeptides were resolved in the chloroplast thylakoid membrane fraction with the most prominent bands which are 59 and 57 KD ($\alpha\;and\;\beta$ subunit of coupling factor: CF) and 26 KD (apoprotein of LHCP). The changes in thylakoid protein profile during 72 h dark incubation showed the rapid degradation in control, but this degradation was prevented in quantity by BA treatment. The above results suggested that BA would inhibit the peroxidation of membrane lipids, thereby preventing the loss of membrane proteins which led to the maintenance of the membrane integrity including chloroplast thylakoid.

• Journal of Nutrition and Health
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• v.34 no.8
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• pp.833-842
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• 2001

The purpose of this study is to determine the effect of dietary proteins and fats on the hepatic histological changes, membrane stability, and drug-metabolizing enzyme activities during chemically induced rat hepatocarcinogenesis. Weanling Sprague-Dawley rats were fed the diet containing 20% casein or soy protein isolate and 15% perilla or corn oil for 10 weeks. Hepatocarcinogensis was initiated with diethylnitrosamine(DEN), and the rats were fed diets containing 0.02% 2-acetylaminofluorene(AAF) followed by 0.05% phenobarbital (PB). The scores of histological changes were decreased in treated rats fed soy protein diet compared to those find casein diet. Liver weights were significantly increased by AAF and PB treatment in rats fed casein diets in both oil groups. Glucose 6-phosphatase(G6Pase) activities, an index of membrane stability, were significantly reduced by AAF and PB treatment in rats find casein diets, and were lower in casein diet compared to soy protein diet groups. Especially, the activities were the highest in the rats fed soy protein-perilla oil diet. Lipid peroxide values also were increased by AAF and PB treatment in rats fed casein diet. Aniline hydroxylase activities were not influenced by protein and fat sources. Glutathione-dependent enzyme activities were increased by AAF and PB treatment. Linoleic and arachidonic acid content were increased in rats fed corn oil diet, and linolenic and eicosapentaenoic acid contents were increased in rats fed perilla oil diet. Our results suggest that soy protein isolate inhibit the abnormal histological changes in liver, possibly by maintaining the membrane stability during chemically induced rat hepatocarcinogenesis. Soy protein may be protective against the hepatocarcinogenesis induced by chemical carcinogen.

• Membrane Journal
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• v.26 no.4
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• pp.266-272
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• 2016

The separation and purification of lysozyme enzyme from chicken egg white (CEW) solution was studied using the dead-end filtration. The optimum operation conditions of the dead-end filtration reveal that the maximum value of permselectivity of lysozyme to the other proteins of ovalbumin and conalbumin in the CEW solution was tested with change of molecular weight cut-off (MWCO) of ultrafitration membrane and pH of the CEW solution. The optimum operation conditions for the efficient permeable separation of lysozyme from the CEW solution are that the membrane MWCO is 30 kD and the pH of CEW solution is 11. At this optimum operation conditions, the maximum value of permselectivity of lysozyme to total proteins in CEW solution is about 83.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.5
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• pp.849-855
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• 1994

Actively growin Excherichia coli(KCTC 1039) cells were treated with paraquat (1, 1'-dimethyl-4, 4'-bipyridili-um dichloride) by cultivating them in the presence of 1.0mM paraquat. The treatment was carried out with or without shaking to understand the effect of oxygen on paraquat action to thebacterial superoxide dismutase (SOd). By the treatment with vigorous shaking , population growth of the organism almostly stopped and specific activities of SOD of the cells drastically decreased. On contrast ot it, the herbicide showed only l limited inhibitory action on bacterial growth and SOD activity by stationary treatment. Proteins prepared from parquat-treated cells divided into two peaks by Sephacryl column chormatogrpahy, while proteins from the intact cells formed a single peak. Cytoplasmic proteins and plasma membrane proteins of intact cells formed separated three peaks by Sephadex G-75 column chormatography. respectively. Among them the second peak disappeared by paraquat treatment , while the third peak became more apparent. Fractions from the first and the third peak showed SOD activity. Paraquat was detected from the same fractions.

• BMB Reports
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• v.34 no.2
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• pp.130-133
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• 2001

The amino acid sequences of 130 kDa and 72 kDa proteins responsible for the larvicidal activity of Bacillus thuringiensis var israelensis (Bti) were analyzed by hydrophobic moment plots. A search for highly amphiphilic $\alpha$-helices was made in these proteins using the helical hydrophobic moment as a criterion of amphiphilicity The protein segments of the largest hydrophobic moments were analyzed. In the present communication we report the surface seeking helices in 130 kDa and 72 kDa proteins of Bacillus thuringiensis var israelensis. It is assumed that the surface seeking segments may participate in one of the membrane-related functions of Bacillus thuringiensis.

• IMMUNE NETWORK
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• v.9 no.2
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• pp.53-57
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• 2009

Engagement of the immunoreceptors initiates signaling cascades resulting in lymphocyte activation and differentiation to effector cells, which are essential for the elimination of pathogens from the body. For the transduction of these immunoreceptor-mediated signals, several linker proteins termed transmembrane adaptor proteins (TRAPs) were shown to be required. TRAPs serve as platforms for the assembly and membrane targeting of the specific signaling proteins. Among seven TRAPs identified so far, LAT and LIME were shown to act as a positive regulator in TCR-mediated signaling pathways. In this review, we will discuss the functions of LAT and LIME in modulating T cell development, activation and differentiation.

• Journal of Mushroom
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• v.15 no.1
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• pp.1-7
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• 2017

Hydrophobins are surface active proteins that are produced by filamentous fungi including mushrooms. Their ability to self-assemble into an amphipathic membrane at any hydrophilic-hydrophobic interface is most intriguing. These small secreted proteins comprise of eight conserved cysteine residues which form four disulfide bridges and an extraordinary hydrophobic patch. Hydrophobins play critical roles in fungal (and/or mushrooms) growth as structural components and in the interaction of fungi and mushrooms with the environment. The biophysical and biochemical properties of the isolated proteins are remarkable, such as strong adhesion, high surface activity and the formation of various self-assembled structures. With the increasing demands of hydrophobins from fungi and mushroom sources, production and purification in large scale is under challenge. Various applications, ranging from food industries, cosmetics, nanotechnology, biosensors and electrodes, to biomaterials and pharmaceuticals are emerging and a bright future is foreseen.

• BMB Reports
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• v.38 no.4
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• pp.381-385
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• 2005

Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus (CoV) that was identified and molecularly characterized in 2003. Previous studies on various coronaviruses indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly and morphogenesis. It is necessary to elucidate the molecular mechanism of SARS-CoV replication and rationalize the anti-SARS therapeutic intervention. In this study, we employed an in vitro GST pull-down assay to investigate the interaction between the membrane (M) and the nucleocapsid (N) proteins. Our results show that the interaction between the M and N proteins does take place in vitro. Moreover, we provide an evidence that 12 amino acids domain (194-205) in the M protein is responsible for binding to N protein. Our work will help shed light on the molecular mechanism of the virus assembly and provide valuable information pertaining to rationalization of future anti-viral strategies.

• Korean Journal of Veterinary Research
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• v.31 no.3
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• pp.259-264
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• 1991

The proteins of the race horse erythrocyte membrane were analysed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate(SDS-PAGE), and their relations to the fast erythrocyte sedimentation rate(ESR) of the race horse were investigated. The erythrocyte sedimentation rate of race horse were very fast compared with the human one(33 times <$90^{\circ}-plastic-ESR/30m$> and 25 times <$90^{\circ}-micro-ESR/30m$> as fast as the human one) are reported previously. Although the general protein profiles of the race horse erythrocyte membranes were almost similar to that of human, band 3 content was showing higher in race horse (34.7%) than in human (25.3%). The glycoprotein profiles of the race horse erythrocyte membranes revealed by periodic acid Schiff's(PAS) stain showed a marked difference from that of human. The PAS-1(glycophorin) and PAS-2(sialoglycoprotein) present in human erythrocyte memo brane were almost absent from the Holstein and race horse erythrocyte membranes, but PAS-2 was more in only race horse from that of human. Instead, the bovine erythrocyte membranes showed a strong PAS-B near the origin of the electrophorograms and the race horse erythrocyte membranes showed a strong PAS-negative band near the end of the electrophorograms, which is named as PAS-E in this study. These results suggest that the fast sedimentation rate of race horse erythrocyte is due in part to the presence of more band 3 protein fraction and PAS-E glycoproteins in the race horse erythrocytes.

• Journal of Microbiology and Biotechnology
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• v.33 no.9
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• pp.1130-1140
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• 2023

Among the AAA+ proteases in bacteria, FtsH is a membrane-bound ATP-dependent metalloprotease, which is known to degrade many membrane proteins as well as some cytoplasmic proteins. In the intracellular pathogen Salmonella enterica serovar Typhimurium, FtsH is responsible for the proteolysis of several proteins including MgtC virulence factor and MgtA/MgtB Mg²⁺ transporters, the transcription of which is controlled by the PhoP/PhoQ two-component regulatory system. Given that PhoP response regulator itself is a cytoplasmic protein and also degraded by the cytoplasmic ClpAP protease, it seems unlikely that FtsH affects PhoP protein levels. Here we report an unexpected role of the FtsH protease protecting PhoP proteolysis from cytoplasmic ClpAP protease. In FtsH-depleted condition, PhoP protein levels decrease by ClpAP proteolysis, lowering protein levels of PhoP-controlled genes. This suggests that FtsH is required for normal activation of PhoP transcription factor. FtsH does not degrade PhoP protein but directly binds to PhoP, thus sequestering PhoP from ClpAP-mediated proteolysis. FtsH's protective effect on PhoP can be overcome by providing excess ClpP. Because PhoP is required for Salmonella's survival inside macrophages and mouse virulence, these data implicate that FtsH's sequestration of PhoP from ClpAP-mediated proteolysis is a mechanism ensuring the amount of PhoP protein during Salmonella infection.