• Food Science and Preservation
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• v.11 no.3
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• pp.417-423
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• 2004

Botanical antimicrobial agent-grapefruit seed extract mixture (BAAG) have an unknown compounds which exhibit the antibiotic activities aganist microorganisms including bacteria and fungi. We have examined the effects of BAAG on the physiological function of Botrytis cinerea which was isolated from necrotic lesions of decayed fruits and vegetables such as cucumbers, grapes, tomatoes, and red peppers during storage. In the results of enzymatic activities related to the energetic metabolism there was no inhibitory effect of BAAG on the activities of several enzymes in vitro including glucose 6-phosphate dehydrogenase and malate dehydrogenase, while there was inhibitory effect of BAAG on the activities of hexokinase and succinate dehydrogenase. O-nitrophenyl-$\beta$-D-galactopyranoside(ONPG), the artificial substrate of $\beta$-galactosidase was hydrolyzed in the presence of BAAG, indicating that the membrane was pertubated by the BAAG. From the results we suggested that the antibiotic activity of BAAG is due to the change of membrane permeability of the cell. BAAG was fractionated and purified by silica gel and sephadex column chromatography. Among active fractions two peaks were identified as naringin and limonin when they were analyzed by by NMR and Fast atomic bombardment.

• Korean journal of applied entomology
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• v.34 no.3
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• pp.181-190
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• 1995

Malate dehydrogenase in the mosquito ovary after a blood meal, Aedes aegypti, was purified and characterized. MDH purification steps involved DEAE-Sepharose, S-Sepharose and Cibacron blue affinity chromatography. The purified MDH was 70,000 daltons in molecular weight and was a homodimer consisting of tow identical subunits. Optimal activity of purified MDH was obtained pH 9.0-9.2 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With obtained pH 9.0-92 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With malate as substrate, purified mitochondrial MDH (1.28$\times$${10}^{-4}$ M) had lower Km value than cytoplasmic MDH (8.92x${10}^{-3}$ M). MDH activity was inhibited by citrate, $\alpha$-ketoglutarate, and ATP. Inhibition of MDH activity by ATP and citrate was less in malate-oxaloacetate reaction and in oxaloacetate-malate reaction. MDH activity was completely inhibited by ATP in oxaloacetate-malate reaction and not inhibited by citrate in malate-oxaloacetate reaction. Temporal activity change of MDH is similar to that of isocitrate dehydrogenase in the ovary after blood feeding; their activities in the ovary began to rise at 18 hours after a blood meal, and reached at the maximal level at 48 hours.

• Korean journal of food and cookery science
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• v.30 no.5
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• pp.613-619
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• 2014

For the development of a hangover soup containing blue mussel, 11 kinds of hot water extracts were prepared - A (mistletoe); B (shepherd's purse); C (arrowroot); D (bean sprout); E (oriental raisin); F (blue mussel); G (blue mussel and mistletoe); H (blue mussel and shepherd's purse); I (blue mussel and arrowroot); J (blue mussel and bean sprout); and K (blue mussel and oriental raisin). Extract C showed the highest effect for increasing the activities of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH); however, the addition of blue mussel did not provide a synergy effect on extract C. Other than the arrowroot-containing extracts (C and I), extract H showed relatively higher ADH ($237.4{\pm}1.7%$) and ALDH ($136.5{\pm}2.1%$) activities. Moreover, extract H showed the highest DPPH radical scavenging activity ($93.9{\pm}0.1%$) and angiotensin I converting enzyme (ACE) inhibitory activity ($42.7{\pm}1.6%$). The combination of blue mussel with shepherd's purse had a synergic effect on its ADH and ACE inhibitory activities.

• Journal of Yeungnam Medical Science
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• v.12 no.1
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• pp.48-55
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• 1995

The present study was designed to evaluate the efficiency of total lactate dehydrogenase, total creatine kinase, LD1/LD2 ratio, CK-MB and newly developed troponin T in acute myocardial infarction. The level of troponin T was $0.01{\pm}0.02{\mu}g/L$ in 34 healthy person, but the peak vaule of acute myocardial infarction ranged in 4.7-24.2 ${\mu}g/L$. Total lactate dehydrogenase was peaked in 1 to 3 days after chest pain and then progressively decreased, but LD1/LD2 ratio was persistently higher than 1.0 for 10 days in most patients. Total creatine kinase and CK-MB were peaked in 1-2 days, and normalized in 3-4 days, so they were useful in early diagnosis of acute myocardial infarction, but not for the late stages of acute myocardial infarction. Troponin T is early elevated and persistently high level for more than 10 days. Comparing with total lactate dehydrogenase, total creatine kinase, LD1/LD2 ratio and CK-MB, troponin-T test improves the efficiency of serodiagnostic method for the detection of ischemic myocardial damage.

• Archives of Pharmacal Research
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• v.20 no.5
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• pp.432-437
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• 1997

We used a herbal medicine, roots of Rhodiola sachalinensis (RS) to assess whether RS extract can decrease blood ethanol concentrations in rats fed ethanol and if so, to elucidate the mechanism by which RS extract reduces blood ethanol levels. Rats were fed ethanol orally 1 hr after the oral administration of various doses of RS extract. In another experiment, rats were injected intraperitoneally with ethanol following the intake of RS extract via gastric catheter to eliminate possible inhibition of ethanol absorption in the gastrointestine by RS extract. The administration of RS extract remarkably lowered blood ethanol levels in a dose-dependent manner in rats given ethanol orally. However, the intake of RS extract did not reduce ethanol levels in rats injected with ethanol intraperitoneally. The activities of two main hepatic enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), involved in ethanol metabolism, were not affected by the administration of RS extract in rats fed ethanol. In addition, the intake of RS extract reduced serum triglyceride levels elevated by ethanol to the normal level. We conclude that the administration of RS extract lowers blood ethanol concentrations by inhibition of ethanol absorption in the gastrointestinal tracts of ethanol-fed animals.

• The Korean Journal of Malacology
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• v.11 no.1
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• pp.51-61
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• 1995

A horizontal starch gal electrophoresis for enzyme proteins extracted from 3 species of Korean planorbid snails; Gyraulus convexiusculus, Hippeutis cantori and Segmentina hemisphaerula was carried out in order to elucidate their genetic relationships.The results from 12 enzymes employed in three different kinds of buffer systems are summarized as follows:1) Two loci from each enzyme of aldehyde oxidase, esterase, glucose phosphate isomerase. isocitrate dehydrogenase, leucine aminopeptidase, malate dehyogenase, peptidase and xanthine oxidase were detected, and only one locus was observed from each of the following four enzymes: 6-phosphogluconate dehydrogenase, glyceraldehyde-phosphate dehydrogenase, glutamate oxaloacetate transaminase and glycerol-3-phosphate dehydrogenase.2) Most of loci in 3 species of planorbid snails employed showed homozygous and monomorphic banding patterns and some of them were specifis as genetic markers among different species. However, a few of loci (EST-1. EST-2 and GPI-2)showed polymorphic banding patterns. 3)Hippeutis cantori and Segmentina hemisphaerula were more closely clustered in a dendrogram with the genetic iddentity value of 0.431, and these two species were lineated with Gyraulus convexiusculus as another cluster at the value of 0.294.In summarizing the above results, three species of Korean planorbid snails employed in this study mostly showed monomorphic enzyme protein banding patterns and genetic differences specific among 3 species.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.85-90
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• 1997

The Isozyme activities of Lentinula edodes were studied as a preliminary study for genetic analysis after protoplast fusion. The presence of peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ was examined. An intracellular buffer-soluble protein from the mycelia was used for enzyme analysis on nondenaturing polyacrylamide gels. The auxotrophs of Lentinula edodes were positive for peroxidase, esterase, superoxide dismutase and acid phosphatase. However, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ were not detected. The esterase and peroxidase were not affected by the various culture age. Isozyme identification may be a useful tool after protoplast fusion.

• Parasites, Hosts and Diseases
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• v.38 no.1
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• pp.45-48
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• 2000

An enzyme analysis of the liver fluke, Clonorchis sinensis from Kimhae, Korea and from Shenyang, China was conducted using a horizontal. starch gel electrophoresis in order to elucidate their genetic relationships. A total of eight enzymes was employed from two different kinds of buffer systems. Two loci from each enzyme of aconitase and esterase (${\alpha}-Na{\;}and{\;}{\beta}-Na$) : and only one locus each from six enzymes, gluucose-6-phosphate dehydrogenase (G6PD), ${\alpha}-glycerophosphate$ dehydrogenase (GPD), 3-hydroxybutyrate dehydrogenase (HBDH), malate dehydrogenase (MDH), phosphoglucose isomerase (PGI), and phosphoglucomutase (PGM) were detected. Most of loci in two populations of C. sinensis showed homozygous monomorphic banding patterns and one of them, GPD was specific as genetic markers between two different populations. However, esterase (${\alpha}-Na$), GPD, HBDH and PGI loci showed polymorphic banding patterns. Two populations of C. sinensis were more closely clustered within the range of genetic identity value of 0.998-1.0. In summarizing the above results, two populations of C. sinensis employed in this study showed mostly monomorphic enzyme protein banding patterns, and genetic differences specific between two populations.

• The Korean Journal of Pharmacology
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• v.17 no.1 s.28
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• pp.33-39
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• 1981

In this paper, the influences of adrenergic neuronal blockades of different mode: guanethidine and ${\alpha}$-methyl-para-tyrosine on the changes induced by carbon tetrachloride $(CCl_4)$ of hepatic total lipid, glycogen, and lipid peroxide contents and serum lactic dehydrogenase activity were investigated in male mice. The results obtained were summarized as follows: 1) The hepatic total lipid and lipid peroxide contents and serum lactic dehydrogenase activity were markedly increased by $CCl_4$, but hepatic glycogen content were decreased. 2) The hepatic total lipid and lipid peroxide contents and serum lactic dehydrogenase activity were not significantly changed by guanethidine(20mg/kg) or ${\alpha}$-methyl-para-tyrosine (5 mg/kg) injection. 3) The increase of hepatic total lipid induced by $CCl_4$ was inhibited by the pretreatment of guanethidine or ${\alpha}$-methyl-para-tyrosine, and the increase of hepatic lipid peroxide content induced by $CCl_4$ was slightly inhibited by them. But the decrease of hepatic glycogen content and the increase of serum lactic dehydrogenase activity induced by $CCl_4$ were not affected by them.

• KSBB Journal
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• v.26 no.3
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• pp.189-192
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• 2011

Much interest has been recently focused on the production of large quantities of hydrogen, due to its potential importance in our economy and needs in the petroleum and chemical industries. Formate dehydrogenase H (FDH-H) from Escherichia coli containing selenocysteine that oxidizes formate to carbon dioxide with the release of hydrogen is a component of the anaerobic formate hydrogen-lyase complex of E. coli. To make full use of FDH-H, we need effective expression condition. In this approach, we investigated the effect of pH on FDH-H stability and observed the effect of selenite and formate concentration on the activity of FDH-H. Additionally, coexpression of selenocysteine insertion genes were tried to improve the expression of FDH-H. The highest level of FDH-H expression was achieved by coexpression of selenocysteine insertion genes (pSUABC) as well as by the addition of $10\;{\mu}M$ selenite and 10 mM formate. At this optimized condition, a 2.6 fold elevation of expression of FDH-H was achieved.