• Applied Biological Chemistry
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• v.32 no.2
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• pp.109-115
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• 1989

This study was aimed to find out the influence of long-term fertilization for 21 years on soil enzyme activities in the silty clay loam textured normal paddy soil. Total urease activity (TUA) and the microbial urease activity (MUA) were shown to be changed significantly, but the accumulated urease activity (AUA) was similar within trial plots. Especially the MUA of the plots annually applied N.P.K. fertilizers with compost and N.P.K. fertilizers with silicate fertilizer were the highest among plots. The total L-glutaminase activity (TGA) and the accumulated L-glutaminase activity(AGA) were changed significantly among trial plots, but the microbial L-glutaminase activity (MGA) was not. By the simple correlation analysis, it was shown that the TGA and the AGA correlated highly significant to available phosphorus available $SiO_2$ content and pH. Addition of the toluene to the incubation mixture did not markedly affect the activity of phosphatase, but the difference of phosphatase activity among plots was significant. By the simple correlation analysis, it was shown that the phosphatase activity ; correlated highly significant to pH, available $SiO_2$, available phosphorus and exchangeable calcium in soils.

• Applied Biological Chemistry
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• v.31 no.3
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• pp.241-248
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• 1988

In order to determine the approptiate usage of insecticides to honeybee(Apis mellifera L.), median effective dose to seven insecticides were studied. $LC_(50)$ value of DDT was the highest as being 58 ppm, and that of EPN was the lowest as being 1.61ppm. Various detoxifying enzymes from the midget cf adult worker bee, including microsomal oxidases, glutathione Stransferases, esterases, and DDT-dehydrochlorinase were assayed. Effects of various insecticides on microsomal enzyme activities were as follows: Aldrin epoxidase activity was inhibited by malathione and permethrin treatment. N-demethylase activity was induced by diazinon and EPN treatment and O-demethlase activity was induced by diazinon treatment. Of the glutathione S-transferases, aryltransferase(DCNB conjugation) activity was significantly induced by diazinon, and moderately induced by permethrin. Of the esterases, ${\alpha}-NA$ esterase activity was moderately inhibited by malatjione and permethrin. Acetylcholinesterase activity was not affected by the sublethal exposure of honeybee to the insecticides. Sublethal exposure of honeybee to the insecticides had no effect on DDT-dehydrochlorinase activity, except carbaryl and permethrin were significantly induced.

• Applied Biological Chemistry
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• v.8
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• pp.75-80
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• 1967

In order to investigate the change of enzyme activities during the fermentation of tobacco leaves, whole and cut leaves were treated for twenty days at $30^{\circ}C$ and $39^{\circ}C$ by the normal procedure and inoculation of yeast, respectively, and the activity of several enzymes was measured at proper intervals. 1) Alpha-amylase activity was steadily decreased with the progress of fermentation. 2) Invertase and catalase activities were steadily decreased until the mid of the period, and then increased again toward the end of the fermentation. The latter enzyme activity showed more marked change than the former. 3) Most of the polyphenol oxidase activity were decreased abruptly in the early stage of the fermentation, and thereafter leveled down slowly. 4) Peroxidase activity was detected throughout the fermentation but no remarkable change was observed. 5) Protease activtty was not detected through the fermentation period.

• Applied Biological Chemistry
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• v.38 no.2
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• pp.174-178
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• 1995

The purpose of this study was to investigate a role of cytochrome $P_{450}$, for the toxicity of the phosalone in in vitro and in vivo bioactivation systems. The bimolecular inhibition rate constants$(k_i)$ of the phosalone to acetylcholinesterase(AChE) and butyrylcholinesterase(BuChE) were approximately $10^2M^{-1}{\cdot}min^{-1}$, respectively, which meant a poor inhibitor. The potency of the phosalone as an inhibitor of AChE and BuChE was increased about 300 and 40 fold, respectively, when the inhibitor and the ChE were incubated with microsomes fortified with NADPH compared with microsome alone. Piperonyl butoxide(PB) addition to these coupled systems greatly reduced the inhibition of both target enzymes by blocking a bioactivation process. The $I_{50}$ value of the Phosalone alone for rat brain AChE was 170 mg/kg. When PB was pretreated, that value was altered to 42.5 mg/kg. PB pretreatment synergized the inhibition of brain AChE with four times. Rat blood erythrocyte AChE and plasma BuChE were similarly inhibited in vivo by the phosalone and PB pretreatment didn't affect significantly the pattern of the inhibition. The in vivo studies showed different results in the role of cytochrome $P_{450}$ from those of the in vitro studies.

• Applied Biological Chemistry
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• v.37 no.3
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• pp.203-209
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• 1994

When $^{14}C-{\alpha}-endosulfan$ was incubated with carp liver, kidney and gut preparations, it was metabolized to water soluble and organosoluble metabolites. In an in vitro test, endosulfan was converted to endosulfan ${\alpha}-hydroxyether$ (EHE), endosulfan alcohol (EA) and endosulfan ether (EE). The addition of NADPH resulted in rapid conversion of endosulfan to the metabolites in 105,000 g soluble fraction and microsomes. However, the rate of metabolism of endosulfan in liver, kidney and gut supplemented with NADPH as a cofactor was higher in the 105,000 g soluble fraction than that in the microsomes of carp under incubation conditions. The enzymes probably involved in the metabolism of endosulfan include the glutathione S-transferase (GST) and the mixed function oxidases (MFO), based on the evidence that addition of either GSH or NADPH increased the degradation of endosulfan.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.55 no.1
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• pp.65-69
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• 2010

This study was carried out to investigate the antioxidative and anti-inflammatory activity of crude anthocyanin compounds extracted from black soybean. The crude anthocyanin compounds were extracted with 80% methanol and concentrated to powder. The most abundant compound isolated from the extract was C3G(cyanidin-3-glucoside). The superoxide dismutase (SOD) assay was conducted to assess the antioxidative activity of the crude extract. SOD, which catalyzes the dismutation of the superoxide anion into hydrogen peroxide and molecular oxygen, is one of the most important antioxidative enzymes. The black soybean anthocyanin extracts inhibited more than 90% of the superoxide radical at a concentration of 0.1% and 100% at a concentration of 0.5%, indicating that this extract displayed excellent antioxidative activity. To assess the anti-inflammatory activity of the extract, a NO(Nitric oxide) production assay in RAW 264.7 cells was performed. NO is an important physiological messenger and effector molecule in many biological systems, including immunological, neuronal and cardiovascular tissues. In this assay, the anthocyanin extracts showed a high anti-inflammatory potential, where the inhibitory potency for NO production was similar to the positive control, particularly for EGCG(epigallocatechin-3-gallate), which is known to have excellent anti-inflammatory activity. Thus, it can be concluded that the anthocyanin extracts from black soybean have distinctive pharmaceutical activities and may be used as an excellent source materials to supplement the health benefits of various food products.

• Journal of Life Science
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• v.17 no.2 s.82
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• pp.230-234
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• 2007

Oxygen is required for many important aerobic cellular reactions, it may undergo electrontransfer reactions, which generate highly reactive membrane-toxic intermediates (reactive oxygen species, ROS), such as hydrogen peroxide, singlet oxygen, superoxide radical, hydroxyl radical, hydroperoxyl radical, hydroxy ion. Various mechanisms are available to protect cells against damage caused by oxidative free radicals, including scavenging enzyme systems such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx). This antioxidant defense system is a very complex and finely tuned system consisting of enzymes capable of detoxifying oxygen radicals as well as low molecular weight antioxidants. In addition, repair and turnover processes help to minimize subcellular damage resulting from free radical attack. $H_2O_2$,one of the major ROS, is produced at a high rate as a product of normal aerobic metabolism. The primary cellular enzymatic defense systems against $H_2O_2$ are the glutathione redox cycle and catalase. From Northern blot analysis of total RNAs from cultured cell with $H_2O_2$ treatment, various results were obtained. Expression of Cu/Zn SOD decreased when cell passage increased, but the level of the Cu/Zn SOD was scarcely expressed in 35 passage.

• Applied Biological Chemistry
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• v.39 no.6
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• pp.472-476
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• 1996

The major portions of two DNA fragments, one from degradative plasmid, pRA4000 from Pseudomonas putida NCIMB 9866, and the other from degradative plasmid, pRA500 from P. putida NCIMB 9869, which harbor the structural genes for the flavoprotein (pchF) and cytochrome (pchC) subunits of p-cresol methylhydroxylase (PCMH), have been sequenced. The DNA and deduced amino acid sequences for pchC and pchF have been published. In these fragments, a coding region (dhal) for an aldehyde dehydrogenase has been identified. It is proposed that this gene encodes for the aldehyde dehydrogenase which converts p-hydroxybenzyaldehyde to p-hydroxybenzoate. p-Hydroxybezealdehyde is the product of oxidation of p-cresol by PCMH. The fragment from P. putida 9869 also harbors the genes for the ${\alpha}$ (pcaG) and ${\beta}$ (pcaH) subunits of protocatechuate 3,4-dioxigenase. The fragment from 9866 does not have any portion of these genes in the corresponding region A possible open reading frame (ORF) between pchC and pchF is seen for both clones, and a second putative open reading frame (ORF') also exists in the 9866 clone. The gene organizations are dhal-pchC-ORF-pchF-pcaGH for the DNA fragment from 9869, and ORF-dhal-pchC-ORF-pchF for the DNA fragment from 9866.

• Applied Biological Chemistry
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• v.39 no.6
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• pp.466-471
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• 1996

The survey on the chitinolytic activity of some plants was performed for the purpose of obtaining some reliable and inexpensive sources of chitinase. Rice, soybean for sprouting, kiwi fruit, almond and crude papain were investigated. Rice bran, seed coat of the soybean and the pericarp of kiwi fruit showed a considerable activity, while the bean after the removal of the seed coat, the mixture of rice integument and endosperm, polished rice, and defatted soybean powder didn't have any detectable activity. These crude enzymes have shown to contain both endo- and exochitinase activity. The effects of pH and temperature on the enzyme activity were variable. Furthermore we have observed the chitosanolytic activity from these enzyme Preparations. The rice bran had the highest activity in the enzymatic degradation of chitosan, and seed coat of soybean and the pericarp of kiwi fruit followed. On the basis of the fact that crude papain was not only commercially available but also the most potent in the endochitinase activity and the lowest in the exochitinase activity, we could conclude that crude papain was considered as the most suitable source of the chitinase among plants studied in this paper. In addition, rice bran was worth further investigation from the point of utilizing agricultural by-product.

• Applied Biological Chemistry
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• v.19 no.3
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• pp.139-144
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• 1976

In order to investigate the properties of enzymes from two strains of mold, reported in the previous paper, (1) studies have been made concerning the characteristics of cellulase of Aspergillus niger-SM6 and Trichoderma viride-SM10, and summarized as follows. 1. In the semi-purification the recovery of ${\beta}-glucosidase$ was the highest when 80-90% ethanol was used and 0.8 saturation of $(NH_4)_2SO_4$. 2. The characteristics of the semi-purified enzyme were as follows. Aspergillus niger-SM6 Trichoderma viride-SM10 Optimum pH 3.5 4.0 pH stability 3.0-6.0 3.0-6.0 Optimum temperature $60^{\circ}C$ $60^{\circ}C$ Heat stability below $60^{\circ}C$ below $50^{\circ}C$ Optimum reaction time 30 min. 60 min. Optimum CMC concentration 3% 3% 3. The Km values of CMCase were 0.8% and 1.01 for Aspergillus niger-SM6 and Trichoderma viride-SM10, respectively. 4. In the strain of Aspergillus niger-SM6, there were high activity of xylanase and pectinase.