• YAKHAK HOEJI
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• v.37 no.6
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• pp.647-658
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• 1993

The susceptibilities of aldehyde dehydrogenase (AldDH) and alcohol dehydrogenase (ADH) to active oxygen generated by xanthine-xanthine oxidase (XOD) system were studied. Incubation of AldDH with 2$\times$10$^{-3}$ units of XOD for 30 min at $25^{\circ}C$ resulted in the decrease of enzyme activity to 30% and it was inactivated completely when incubated with 5$\times$10$^{-3}$ units of XOD. Whereas 70% of ADH activity was retained after exposure to 5$\times$10$^{-3}$ units of XOD for 30 min, 40% of ADH activity was retained after exposure to 5$\times$10$^{-2}$ unit of XOD for 30 min. This inhibition effect by the active oxygen was preventable by catalase and glutathione, but not by SOD. The rates of the NADPH-dependent oxygen consumption by the liver S-9 mixture and microsomes were also determined in this study. Rate of oxygen consumption is increased in the liver S-9 mix and microsomes from phenobarbital-treated rat, and it was consistent with increased lipid peroxidation. In the presense of ethanol as a substrate, the oxygen consumption rates were increased. It is reported that hepatic AldDH activity is depressed in alcoholic liver diseases, however there is few report that explains the reason of depressed AldDH activity. These results are supportive of the theory that the increase in hepatic ethanol oxidation through the induced ME activity after chronic ethanol feeding generate oxygen radical at elevated rates and it leads to the depression of AldDH activity.

• Asian-Australasian Journal of Animal Sciences
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• v.2 no.3
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• pp.491-492
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• 1989

• Microbiology and Biotechnology Letters
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• v.24 no.3
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• pp.268-273
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• 1996

An extremely cadmium tolerant yeast, Hansenula anomala B-7 used to determine the modification of the intracellular enzyme activities by cadmium ion. The activities of alcohol dehydrogenase, phosphofructokinase, and cytidine deaminase were decreased up to 90%, 40%, and 86% compa- red with the control by 1 mM cadmium nitrate respectively, but the activities of malate dehydrogenase, 6- phosphogluconate dehydrogenase, cytochrome c oxidase, and alkaline phosphatase were increased up to 440%, 136%, 260% and 155% compared with the control by 1 mM cadmium nitrate respectively. These results show that the activities of the enzymes participating in Embden-Mayerhof pathway (e.g. anaerobic metabolism) were reduced by cadmium, but those involved in hexose monophosphate pathway and tricarboxylic acid cycle (e.g. aerobic metabolism) were stimulated in contrast. It has been suggested that the diminished activity of cytidine deaminase in pyrimidine nucleotide dissimilation occured due to the inhibited nucleotide dissimilation by cadmium ion; the enhanced activity of cytochrome c oxidase was specifically required in order to oxidize a raised amount of NADH and NADPH due to the increased aerobic metabolism.

• Advances in Traditional Medicine
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• v.9 no.4
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• pp.303-306
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• 2009

The defatted methanol extract of Raphanus sativus Linn. (Cruciferae) seed (MERS) was evaluated for its antisteroidogenic potential in mature female Swiss albino mice. The methanol extract at the doses of 100 and 200 mg/kg body weight significantly elevated the levels of cholesterol and ascorbic acid contents which serve as a precursor for the synthesis of steroid hormones in ovaries. The extract also significantly inhibited glucose-6-phosphate dehydrogenase and ${\Delta}^5-3{\beta}$-hydroxy steroid dehydrogenase, the two key enzymes involved in ovarian steroidogenesis. Hence the extract (MERS) exhibited significant antisteroidogenic activity.

• The Korean Journal of Zoology
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• v.34 no.1
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• pp.123-130
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• 1991

Several parameters of u -glycerol-3-pholphate dehydrogenase (GPDH) such as activity, content and translatable mRNA levels were measured to elucidate mechanism underlving developmental and tissue specific regulation of 6PDH activity in Drosophila melonogastrr. In adult segments, most of total GPDH activity (62%1 Iwas detected in thorax where GPDH-1 resided, while 32% of total GPDH aUiviD was only detected in abdomen where GPDH-3 resided. The relative synthesis of GPDH was, however, similar in both tissues, although 58% of total GPDH was synthesized in abdomen. These results strongly suggest that the turnover rate of the abdominal enzyme (GPDH-3) was much more rapid than that of thoracic enzymes (GPDH-1). In nitro translation and immunoblotting experiments also indicate that GPDH-3 was arised by posttranslational modification from a single polypeptide (GPDH-1).

• Environmental Analysis Health and Toxicology
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• v.16 no.1
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• pp.9-16
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• 2001

It is known that alcoholics have significantly lower mitochondrial aldehyde dehydrogenase (ALDH)s'activity than do normal subjects or nonalcoholics with liver disease. However, there are only few reports that explain the reasons behind this reduction of ALDHs'activities. In this study, ALDH activity is inhibited by acetaldehyde, a substrate for ALDH However, the addition of glutathione (GSH) protected ALDH activities against the inhibitory effects of acetaldehyde in vitro. Furthermore, when GSH depletion is induced using diethyl maleate (DEM) in rats by 24% in cytosol and 43% in mitochondria, ALDH activities were also depressed by 31% and 63%, respectively compared to non-treated rats without significant reductions in other hepatic enzymes. These results suggest that ALDHs'activities are closely related to the concentration of acetaldehyde and/or cellular GSH contents . Therefore in alcoholic liver disease, increased productions of acetaldehyde and decreased contents of mitochondrial GSH may involved in the depression of ALDHs'activities.

• YAKHAK HOEJI
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• v.45 no.5
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• pp.500-505
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• 2001

Puerariae Radix is one of the medicinal plants used in oriental medicine for hangover, It has been claimed for several pharmacological effects including anti-alcohol abuse, antidipsotropic activity and anti-alcohol intoxication. In connection with Puerariae Radix effects, an activity-guided purification of active substance on alcohol dehydrogenase (hnH) was carried-out. The most active compound was isolated as puerarin (C$_{21}$H$_{20}$ O$_{9}$ ), molecular weight 416. Puerarin inhibited ADH noncompetitively against ethanol or NAD$^{+}$./.

• Korean Journal of Microbiology
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• v.31 no.3
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• pp.214-217
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• 1993

Carbon monoxide dehydrogenase (CO-DH) was found to be present in Acinetobacter sp. strain JC1 grown on CO and also on methylotrophic and heterotrophic substrates, except for pyruvate and nutrient broth. The amounts of CO-DH in cells grown on methylamine, glucose, galactose, and succinate were comparable to that of the CO-grown cells. CO-DH activity, however, was onot deteted by the dye-linked assay method in cell extracts prepared from cells grown on organic substrates, except on ethanol and succinate. THe activity was detected when the CO-DH was stained by activity using CO as a substrate. CO-DHs in cells grown on different substrates were found to be identical in immunological properties.

• Journal of Physiology & Pathology in Korean Medicine
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• v.18 no.6
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• pp.1723-1727
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• 2004

We investigated the activity and stability of alcohol dehydrogenase from horse liver (HLADH) under the electric stimulation. The activity and stability of alcohol dehydrogenase depended on electric output voltaqe, stimulation time, pulse duration and pulse interval, and temperature. HLADH retained about 23% of its activity in buffer but 78% in 10% trehalose solution under electric stimulation with 10V, 10min, The stabilizing of enzymes against electric stimulation by stabilizing additives showed a great potential use of enzymes in biotechnology and medical engineering fields.

• Journal of Microbiology
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• v.35 no.1
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• pp.30-39
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• 1997

Acinetobacter sp. strain JC1 DSM 3803, a carboxydobacterium, was found to grow methylotrophically at the expense of methanol and methlamine, but not of methane, formaldehyde, formate, dimethylamine, or trimethylamine, as the sole source of carbon and energy. The doubling times of the bacterium growing on methanol (0.5%, v/v) and methylamine (0.5%, w/v) at 3$0^{\circ}C$ and pH 6.8 were 4.8 h and 5.7 h, respectively. Cells grown on methanol, however, failed to show typical methanol dehydrogenase and oxidase activities. The cell was found to contain no c-type cytochromes. Cells grown on methanol exhibited higher catalase activity than those grown on pyruvate or glucose. The catalase present in the cells also exhibited peroxidase activity. The catalase activity, growth on methanol of the cell, and oxygen consumption by methanol-grown maldehyde dehydrogenase, formaldehyde reductase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase activities were detected from cells grown on methanol.