• Korean Journal of Environmental Agriculture
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• v.25 no.2
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• pp.174-179
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• 2006

Chinese cabbage, Braccica campestris has long been consumed as a staple food for Koreans in various forms of fresh, salted, and fermented Kimchi. Cultivation of the crop under greenhouse has become a general practices to fulfill its off-seasonal consumer's demand. However, agricultural practices of the crop have always accompanied with heavy applications of pesticides caused by severe outbreaks of diseases and pose under warm and humid circumferences. Since dissipation patterns of pesticide residues in/on the crop under greenhouse conditions ate quite different from those in the open-air, changes of diazinon, O,O-diethyl O-2-isopropyl-6-methylpyrimidin-4-yl phosphornthioate, in/on the Chinese cabbage applied by foliar spraying under greenhouse were studied. Diazinon 34% EC was applied with dilution of recommended and double dose to the crop. The shoots of crop were harvested immediately after this application and at regular intervals over a 10-day. After sample preparations, the diazinon residue was analyzed using gas chromatography equipped with electron capture detector (GC/ECD). Initially deposited amount of the chemical in/on the crop right after applications with recommended and double doses were 8.3 and 15.2 mg/kg, respectively. The residue levels after 10 days of application were 0.03 and 0.09 mg/kg with 1.3 and 1.5 days of half-life in/on the crop, respectively. In consequent 10 days of pre-harvest interval (PHI) for diazinon EC formulation in/on Chinese cabbage under greenhouse condition was fulfill maximum residue level set by Korea Food and Drug Administration (KFDA, 0.1 mg/kg).

• Microbiology and Biotechnology Letters
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• v.33 no.3
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• pp.184-188
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• 2005

IgE-dependent histamine-releasing factor (HRF) is found extracellularly to regulate the degranulation process of histamine in mast cells and basophils and known to play a predominant role in the pathogenesis of chronic allergic disease. HRF has been also identified in the intracellular region of the cell. Previously, we reported that HRF interacts with the 3rd cytoplasmic domain of the alpha subunit of Na,K ATPase and inhibits Na,K-ATPase activity. The predicated phosphorylation site in HRF by PKC was mapped to one serine residues (S98) by the computer analysis. In this study, we identified that S98 residue of HRF was phosphorylated using anti-HRFpS98 antibody which specifically recognizes the phosphorylated serine residue of HRF and HRFS98A mutant construct. We also performed $^{86}Rb^{+}-uptake$ assay to understand the role of HRF wild-type and HRFS98A mutants on the regulation of Na,K-ATPase activity. Dephosphorylation of HRF at serine 98 residue recovers slightly the inhibitory function of HRF, suggesting that phosphorylated HRF at serine 98 may not suppress the Na,K-hfpase activity.

• Journal of fish pathology
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• v.9 no.2
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• pp.157-168
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• 1996

In this study, Residue of formaldehyde and histopathological changes in formalin and neutralformalin in treated fish(Sebastes schlegeli) were observed at two different temperatures(15 and $25^{\circ}C$). Immediately after in treatment, residue of formaldehyde in formalin treated fish was show little bit higher than in neutral-formalin treated fish at $15^{\circ}C$. But, there is no difference at water temperature $25^{\circ}C$. The elimination of formaldehyde was markedly temperature-dependent. The approximated withdrawal time were 72hr and 24hr at water temperature 15 and $25^{\circ}C$. Formalin was more toxic than the neutral-formalin at the same condition. Intensity of tissues damage was increased with increasing concentration of chemical and temperature. Formalin and neutral-formalin treatments caused edema and seperation of epithelium, winding of secondary gill lamella, necrosis in the gill ; congestion and pycnosis, vacuolation in the liver ; hydropic and granulated degeneration, necrosis of epithelial cells in the proximal renal tubule ; increasing mucus cells, cracking, necrosis of epidermis and dermis in the skin tissue.

• The Korean Journal of Food And Nutrition
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• v.10 no.1
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• pp.92-96
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• 1997

A Korean commercial sweet rice drink "Sikhye" showed sucrose, fructose, glucose, maltose, limit dextrin and various size of maltooligosaccharides in HPLC and TLC analysis. Commercial Sikhye was found to contain 0.09% of limit dextrin and 0.2% of rice residue. Limit dextrin in commercial Sikhye showed both signal of $\alpha$-1,4- and $\alpha$-1,6-glucosidic linkage with its estimation ratio of 15:1 by 1H-NMR analysis. This limit dextrin was hydrolyzed to produce various size of maltooligosaccarides with more longer chain than that of traditional Sikhye by pullulanase. Limit dextrin was digested wit enzymes(30units/ml) of $\alpha$-amylase, $\alpha$-glucosidase and glucoamylase from Aspergillus awamori, sweet potato $\beta$-amylase and human salivary $\alpha$-amylase at 37$^{\circ}C$ for 1 hour, respectively. Hydrolysis rates of these amylases on it were higher than in case of traditional sikhye. $\alpha$-Glucosidase plus human salivary $\alpha$-amylase hydrolyzed it to 61.3%. Hydrolysis rates of these amylases on rice residue were lower than that of traditional Sikye. These results suggest that limit dextrin in commercial Sikhye is less effective than isomaltooligosaccharides in traditional Sikhye as a growth factor for Bifidobacterium while rice residue in commercial Sikhye is more effective than that in traditional Sikhye as dietary fiber.ary fiber.

• Korean Journal of Food Science and Technology
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• v.26 no.5
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• pp.603-608
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• 1994

This study was undertaken to find out the effect of phytate on the protein digestibility of various soybean foods, including soy milk, bean curd, curd residue, cheongkukjang, soy sauce, and soy paste. The phytate content of soybean was 2.4%, which decreased to 0.2%, 0.7%, and 0.4% in soy milk, bean curd, and curd residue, respectively, and to 0.2% and 1.0% in soy sauce and soy paste, respectively. The phytate/protein ratio was not correlated with protein digestibility by pepsin whereas the ratio was highly correlated with pancreatin digestibility (p<0.01, r= -0.73). According to SDS-PAGE for the soluble protein fractions, soaked bean showed an alteration in soluble components and bean curd residue exihibited newer low molecular weight bands. Fermented soy products showed no protein band, likely due to degradation.

• KSBB Journal
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• v.19 no.2
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• pp.159-163
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• 2004

The X-ray structure of the cydodextrin-glucanotransferase of Bacillus macerans was solved by molecular replacement at 2.0 ${\AA}$ resolution. The refined structure has a crystallographic R-factor of 16.6%, (R$\sub$free/ = 20.5%). A new metal binding site occupied by two Ca$\^$2+/-ions was found at an accession channel of the active site. There is a large accumulation of negative charges that bind these Ca$\^$2+/-ions, thereby connecting segment ${\beta}$13-${\alpha}$G (residue 254-276) to the main body of domain A (at ${\alpha}$H, residue 283-297). The segment 313-${\alpha}$G contains the catalytic residue Glu258 between subsite 1 and -1 and Tyr260 (subsite 2) which is located at the entrance of the active site. The Ca$\^$2＋/-site 3a,b may have a major role for the activity and specificity of this CGTase, although it is not even conserved for the a-subclass of CGTases.

• Genomics & Informatics
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• v.12 no.2
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• pp.71-75
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• 2014

The tRNA structure contains conserved modifications that are responsible for its stability and are involved in the initiation and accuracy of the translation process. tRNA modification enzymes are prevalent in bacteria, archaea, and eukaryotes. tRNA Gm18 methyltransferase (TrmH) and tRNA $m^1G37$ methyltransferase (TrmD) are prevalent and essential enzymes in bacterial populations. TrmH involves itself in methylation process at the 2'-OH group of ribose at the 18th position of guanosine (G) in tRNAs. TrmD methylates the G residue next to the anticodon in selected tRNA subsets. Initially, $m^1G37$ modification was reported to take place on three conserved tRNA subsets ($tRNA^{Arg}$, $tRNA^{Leu}$, $tRNA^{Pro}$); later on, few archaea and eukaryotes organisms revealed that other tRNAs also have the $m^1G37$ modification. The present study reveals Gm18, $m^1G37$ modification, and positions of $m^1G$ that take place next to the anticodon in tRNA sequences. We selected extremophile organisms and attempted to retrieve the $m^1G$ and Gm18 modification bases in tRNA sequences. Results showed that the Gm18 modification G residue occurs in all tRNA subsets except three tRNAs ($tRNA^{Met}$, $tRNA^{Pro}$, $tRNA^{Val}$). Whereas the $m^1G37$ modification base G is formed only on $tRNA^{Arg}$, $tRNA^{Leu}$, $tRNA^{Pro}$, and $tRNA^{His}$, the rest of the tRNAs contain adenine (A) next to the anticodon. Thus, we hypothesize that Gm18 modification and $m^1G$ modification occur irrespective of a G residue in tRNAs.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.2
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• pp.158-161
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• 2005

We have isolated fractions from Cordyceps militaris and Paecilomyces japonica and investigated their effects on the activity of rat liver cytosolic glucokinase, a key metabolic enzyme involved in carbohydrate metabolism. The dried powder of the C. militaris and P. japonica were successively extracted with ethanol and with 70% ethanol. The residue was exhaustively extracted with hot water. The extract was dialyzed against water, and to the non-dialyzable solution was added 2 volumes of ethanol. The precipitate was collected by centrifugation dispered in water, and lyophilized to afford fraction A. The residue after hot-water extraction was suspended in 5% sodium carbonate. The final residue was suspended in 5% NaOH. The alkaline suspension was purified in a similar manner as described above to afford fraction B. Hepatic glucokinase activities of the fraction A extracted from C. militaris and P. japonica were 371.4 and 379%, respectively. The fraction B was 314.2 and 147.4%. The activity of fraction B of C. militaris extracts was higher than that of P. japonica. Liver cytosolic glucokinase activity of rats fed normal diet supplemented with 0.1% C. militaris was 1316%. In conclusion, the present study has demonstrated that C. militaris extracts were able to prevent sudden postprandial peaks in blood glucose as a result of a marked increase in the liver cytosolic glucokinase activities.

• ETRI Journal
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• v.16 no.1
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• pp.45-57
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• 1994

The effects of reactive ion etching (RIE) of $SiO_2$ layer in $CHF_3/C_2F_6$ on the underlying Si surface have been studied by X-ray photoelectron spectroscopy (XPS), secondary ion mass spectrometer, Rutherford backscattering spectroscopy, and high resolution transmission electron microscopy. We found that two distinguishable modified layers are formed by RIE : (i) a uniform residue surface layer of 4 nm thickness composed entirely of carbon, fluorine, oxygen, and hydrogen with 9 different kinds of chemical bonds and (ii) a contaminated silicon layer of about 50 nm thickness with carbon and fluorine atoms without any observable crystalline defects. To search the removal condition of the silicon surface residue, we monitored the changes of surface compositions for the etched silicon after various post treatments as rapid thermal anneal, $O_2$, $NF_3$, $SF_6$, and $Cl_2$ plasma treatments. XPS analysis revealed that $NF_3$ treatment is most effective. With 10 seconds exposure to $NF_3$ plasma, the fluorocarbon residue film decomposes. The remained fluorine completely disappears after the following wet cleaning.

• Food Science and Preservation
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• v.10 no.3
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• pp.360-364
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• 2003

This study was conducted to investigate the preparation possibility of Beni-koji by Monascus pilosus using dried soybean curd residue(Biji). The additional effect of water(0-50％), glucose(0-10％, w/w), monosodium glutamate(0-0.l％, w/w) and citrus peel water extracts (0-0.5％, v/w) on the pigment and monacolin K content of the Biji Beni-koji were examined. Optimal added amounts of water was 20％ of dried Biji. The highest pigment content(OD at 500 nm) of Biji Beni-koji was 1.06 in 10％ glucose, 2.26 in 0.01％ monosodium glutamate and 2.61 in 0.4％ citrus peel water extracts. The content of monacolin K in the Biji Beni-koji added with 10％ glucose, 0.01％ monosodium glutamate and 0.4％ citrus peel water extracts showed 96.38 mg％(w/w), 118.25 mg％(w/w) and 104.50 mg％(w/w), respectively.