• Journal of Plant Biology
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• v.34 no.1
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• pp.53-57
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• 1991

The effect of polyamines and methylglyoxal bis(guanylhydrazone)(MGBG) on the activity of diamine oxidase was studied in soybean (Glycine max) seedlings. $10^{-2}\;M$ of putrescine, spennidine, and spermine inhibited diamine oxidase activity, whereas $10^{-6}\;M$ putrescine increased enzyme activity. These results suggest that diamine oxidase can be induced by a specific substrate, putrescine. The content of putrescine was increased in response to the increase in concentratioin of MGBG. In vitro, 40% of the diamine oxidase activity was inhibited by $10^{-3}\;M$ MGBG. In vivo, the diamine oxidase activity was increased by a low concentrration of MGBG. It was suggested that MGBG inhibited the formation of spermidine and that the accumulated putrescine induced diamine oxidase, whereas the diamine oxidase acitivity was inhibited by a high concentration of MGBG. It is suggested that a high cocentration of MGBG increases the putrescine content by inhibiting diamine oxidase activity which is responsible for putrescine degradation.dation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.3
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• pp.209-213
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• 1991

To evaluate the effect of methanethiol on the activity of xanthine oxidase in both liver and serum, the rats intraperitoneally received methoanethiol. Injection of methoanethiol in rats showed the more decreased xanthine oxidase activity of boty liver and serum than that of the control group. Concomitantly, the xanthine oxidase activity in livers preincubated with methanethiol was decreased in vitro. The xanthine oxidase in livers preincubated with the methoanethiol also showed more increased Km and similar Vmax value than those of the control. These results suggest that the methanethiol may induce a change in substrate binding affinity of xanthine oxidase.

• Journal of Life Science
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• v.16 no.5
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• pp.866-869
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• 2006

The inhibitory effect of pine needle (Pinus densiflora S.) on potato polyphenol oxidase (PPO) was investigated. The addition of the pine needle extract exhibited a higher inhibitory effect on the potato polyphenol oxidase activity than that of the citric acid or potassium sorbate. The enzyme activity was strongly inhibited in a pH range of 7.0-8.0. When the incubation time of reaction mixture was increased, the potato polyphenol oxidase activity was markedly inhibited. The pine needle extract inhibited the potato polyphenol oxidase non-competitively. And also the pine needle extract subjected to a heat treatment at $100^{\circ}C$ for 10 min or to an acid treatment at pH 2.0, 3.0, and 4.0 for 3 hours still retained inhibitory effect on potato polyphenol oxidase.

• Journal of Microbiology
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• v.40 no.2
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• pp.125-128
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• 2002

The aerobic respiratory chain of Vibrio alginolyticus possesses two different kinds of NADH oxidase systems, i.e., an $Na^{+}$-dependent NADH oxidase system and an $Na^{+}$-independent NADH oxidase system. When deamino-NADH, which is the only substrate for the $Na^{+}$-dependent NADH oxidase system, was used as a substrate, the maximum activities of $N^{+}$-dependent NADH: quinone oxidoreductase and $Na^{+}$-dependent NADH oxidase were obtained at about 0.06 M and 0.2 M NaCl, respectively. When NADH, which is a substrate for both $Na^{+}$-dependent and $Na^{+}$-independent NADH oxidase systems was used as a substrate, the NADH oxidase activity had a pH optimum at about 8.0. In cGntrastl when deamino-NADH was used as a substrate, the NADH oxidase activity had a pH optimum at about 9.0. On the other handle inside-out membrane vesicles prepared from the wild-type bacterium generated only a very small $\Delta$pH by the NADH oxidase system, whereas inside-out membrane vesicles prepared from Napl, which is a mutant defective in the $Na^{+}$ pump, generated $\Delta$pH to a considerable extent by the NADH oxidase system. On the basis of the results\ulcorner it was concluded that the respiratory chain-linked components of V. atginotyticus affect each other.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.797-802
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• 1993

The properties of the alcohol-oxidase from yeasts assimilating of methanol(Hansenula polymorpha CBS 4732, Pichia pastoris CBS 2612 and Candida boidinii CBS 8106) as free(cellules, purified enzymes) and immobilized forms(immobilized cellules, immobilized enzymes) were investigated. Immobilization enhanced the activity and stability of alcohol-oxidase to a certain degree. The optimum temperature of the immobilized alcohol-oxidase was lower than those of the free forms. The pH / activi쇼 profiles of alcohol-oxidase did not change by immobilization, but changed by the microorganisms. When the immobilized cellules were stocked at 4$^{\circ}C$ in 10mM potassium phosphate buffer(pH 7.5 or 8.0), alcohol-oxidase was more stable than those were stocked in potassium phosphate buffer containing 0.65M sucrose. The immobilization modifies the conditions of oxidation on the various substrates. alcohol-oxidase in immobilized forms showed some with higher Km value for methanol than that in free ones.

• YAKHAK HOEJI
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• v.39 no.5
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• pp.521-527
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• 1995

This study was done to determine the effect of lead acetate on the activities of the hepatic cytosofic xanthine oxidase and aldehyde oxidase which were well known as oxygen free radical generating enzyme in vitro. Lead ion accelerated the formation of lipid peroxide and the increment of xanthine oxidase(type O) activity and the type conversion ratio from xanthine dehydrogenase to xanthine oxidase dose-dependently. But xanthine dehydrogenase(type D) activity was decreased. Aldehyde oxidase activity was not changed by lead ion. These data suggested that lead-induced cellular to)dcity may be concerned partially with xanthine oxidase mediated lipid peroxidation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.4
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• pp.418-422
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• 1993

For the purpose of utilizing tannins in the functional foods and crude drugs the xanthine oxidase inhibition of tannins isolated from Korean green tea was determined. Acetone extract from Korean green tea showed inhibitory effect against the xanthine oxidase. The galloyl tannins showed higher inhibitory activity against xanthine oxidase than the nongalloyl tannins. In terms of stereo isomers, (-)-epicatechins had higher inhibitory activity than the (+)-catechins. The synergistic activity was also observed. Tannins isolated from Korean green tea appeared to be incompetitive inhibitor against the xanthine oxidase.

• BMB Reports
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• v.29 no.4
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• pp.300-307
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• 1996

ATP and ADP are potential regulators of mitochondtial respiration and at physiological concentrations they affect the rate of electron transfer between cytochrome c and cytochrome c oxidase. The electron transfer, however, depends on the electrostatic interaction between the two proteins. In order to exclude any nonspecific ionic effects by these polyvalent nucleotides, we used 2'-O-(2,4,6)trinitro(TNP)-derivatives of ATP and ADP which have three orders of magnitude higher affinity for cytochrome c oxidase. A simple titration of the fluorescence intensity of TNP by cytochrome c oxidase showed a binding stoichiometry of 2:1 cytochrome c:cytochrome c oxidase. Higher ionic strength was required for TNP-ATP than for TNP-ADP to be dissociated from cytochrome c oxidase, indicating that the negative charges on the phosphate group are at least partially responsible for the binding. In both spectrophotometric and polarographic assays, addition of ATP (and ADP to a less extent) showed an enhanced cytochrome c oxidase activity. Both electron paramagnetic resonance and fluorescence spectra indicate that there is no Significant change in the cytochrome c-cytochrome c oxidase interaction. Instead, reduction levels of the cytochromes at steadystate suggest that the increased activity of nucleotide-bound cytochrome c oxidase is due to faster electron transfer from cytochrome ${\alpha}$ to cytochrome ${\alpha}_3$, which is known to be the fate limiting step in the oxygen reduction by cytochrome c oxidase.

• Proceedings of the KIEE Conference
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• 1999.11d
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• pp.984-986
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• 1999

In the case of immobilizing of glucose oxidase in organic polymer using electrosynthesis, the glucose oxidase obstructs charge transfer and mass transport during the film growth. This may lead to short chained polymer and make charge-coupling weak between the glucose oxidase and the backbone of the polymer. That is mainly due to insulating property and net chain of the glucose oxidase. Such being the case, it is useless to increase in amount of glucose oxidase more than reasonable in the synthetic solution. We establish by means of qualitative analysis that amount of immobilized glucose oxidase can be improved by adding a hole ethyl alcohol in the synthetic solution. As ethyl alcohol was added by 0.1mol $dm^{-3}$ in the synthetic solution, the faradic impedance of resultant electrode was increased about five times as much as the case of ethyl alcohol free in the solution, and mass transport was limited more than over. That is due to insulating property and net chain of the glucose oxidase. Moreover, in ultraviolet spectra of the synthetic solution, the adsorption peak at 285nm corresponding to glucose oxidase was decreased. It suggests increase in amount of immobilized glucose oxidase.

• Journal of Microbiology
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• v.44 no.3
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• pp.284-292
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• 2006

The cbb3 cytochrome c oxidase has the dual function as a terminal oxidase and oxygen sensor in the photosynthetic bacterium, Rhodobacter sphaeroides. The cbb3 oxidase forms a signal transduction pathway together with the PrrBA two-component system that controls photosynthesis gene expression in response to changes in oxygen tension in the environment. Under aerobic conditions the cbb3 oxidase generates an inhibitory signal, which shifts the equilibrium of PrrB kinase/phosphatase activities towards the phosphatase mode. Photosynthesis genes are thereby turned off under aerobic conditions. The catalytic subunit (CcoN) of the R. sphaeroides cbb3 oxidase contains five histidine residues (H2l4, B233, H303, H320, and H444) that are conserved in all CcoN subunits of the cbb3 oxidase, but not in the catalytic subunits of other members of copper-heme superfamily oxidases. H214A mutation of CcoN affected neither catalytic activity nor sensory (signaling) function of the cbb3 oxidase, whereas H320A mutation led to almost complete loss of both catalytic activity and sensory function of the cbb3 oxidase. H233V and H444A mutations brought about the partial loss of catalytic activity and sensory function of the cbb3 oxidase. Interestingly, the H303A mutant form of the cbb3 oxidase retains the catalytic function as a cytochrome c oxidase as compared to the wild-type oxidase, while it is defective in signaling function as an oxygen sensor. H303 appears to be implicated in either signal sensing or generation of the inhibitory signal to the PrrBA two-component system.