• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.663-667
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• 1996

Acid phosphatase (EC 3.1.3.2) from Welsh onion was partially purified by Sephacryl S-200 gel filtration and CM-Sepharose CL-6B ion exchange chromatography. The optimum pH and temperature of acid phosphatase from green onion were pH 5.5 and $60^{\circ}C$, respectively. The enzyme was the most stable at pH 6.0 and unstable above pH 9.0. The activation energy of the enzyme was determined to be 4.86kcal/mole. The enzyme utilized p-nitrophenyl phosphate most as a best substrate among tested possible substrates, while 5'-GMP and 5'-IMP were poor substrates for the enzyme. $K_{m.app.}$ of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.87mM. Among metal ions and inhibitors tested, $Cr^{+++},\;Zn^{++},\;Cu^{++}$, molybdate and metavanadate ions inhibited the enzyme reaction drastically.

• Journal of The Korean Society of Grassland and Forage Science
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• v.33 no.3
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• pp.153-158
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• 2013

Molybdenum (Mo) in rhizosphere influences sulfate assimilation as well as a number of other physiological aspects. In this study, the activity of key enzymes in sulfate assimilatory pathways, such as ATP sulfurylase (ATPs), adenosine 5'-phosphosulphate reductase (APR), as well as the responses of reactive oxygen species (ROS), were analyzed to elucidate the metabolic and physiological effects of external Mo supply to detached leaves of Trifolium repens L. Mo supply with a range from 1 mM to 40 mM depressed the activity of ATPs throughout the entire time course. In the leaves exposed to 1 mM Mo, a continuous decrease in the activity of ATPs was confirmed by Native-PAGE. The APR activity was also declined by Mo treatment. The accumulation of $H_2O_2$ and ${O_2}^{{\cdot}-}$ were not significant up to 10 mM Mo, whereas a remarked accumulation was detected under 40 mM Mo supply. The data suggest that an external supply of Mo has an inhibitory effect on sulfate assimilation, and induces oxidative stress only at an extremely high concentration.

• The Journal of Korean Institute of Electromagnetic Engineering and Science
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• v.30 no.6
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• pp.445-451
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• 2019

This paper presents the design of a water-cooled radio-frequency(RF) load with simple structure, for use in the ultrahigh-frequency (UHF) band. After establishing a formula to obtain the physical properties that affect RF matching, we measure the permittivity and $tan{\delta}$(Loss tangent) of tap water. Because the temperature of tap water increases upon applying high power, we measure the permittivity and $tan{\delta}$ for all changes in the temperature of tap water. In order to reduce the length of the water-load, molybdate with high $tan{\delta}$ is mixed with tap water. The loss tangent of the mixture is found to be approximately 26 times higher than that of tap water. Finally, we manufacture a water-cooled RF load and measure its characteristics. A reflection coefficient of -19 dB and bandwidth of 15 % is obtained at 460 MHz.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.490-495
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• 1994

Acid phosphatase (EC3.1.3.2) from carrots was partially purified by ammonium sulfate fractionation (30%-80%), Sephacryl S-200 gel filtration, cm-Sepharose CL-6B and DEAE -Sephacel ion exchange chromatography. The optimum ph and temperature of acid phosphatase from carrots were pH 5.5 and 55$^{\circ}C$, respectively. The enzyme was most stable at ph 6.0 and relatively unstable below pH 4.0 . The activation energy of the enayme was determined to be 10.6kcal/mole. The enzyme utilized p-nitrophenyl phosphate as a substrate among tested possible substrates, whereas it hydrolyzed 5' -IMP and 5'-GMP poorly. The Michaelis -Menten constant(Km) of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.55mM. Amongtested metal ions and inhibitors, Al+++ Zn++, Cu++ , fluoride, metavanadate and molybdate ions inhibited the enzyme activity drastically.

• Journal of Microbiology and Biotechnology
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• v.19 no.9
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• pp.918-921
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• 2009

In the present study, we examined the inhibitory effects of protein tyrosine phosphatase (PTPase) inhibitors, including sodium orthovanadate (SOV), ammonium molybdate (AM), and iodoacetamide (IA), on cell growth, accumulation of astaxanthin, and PTPase activity in the photosynthetic algae Haematococcus lacustris. PTPase activity was assayed spectrophotometrically and was found to be inhibited 60% to 90% after treatment with the inhibitors. SOY markedly abolished PTPase activity, significantly activating the accumulation of astaxanthin. These data suggest that the accumulation of astaxanthin in H. lacustris results from the concerted actions of several PTPases.

• Journal of the Korean Chemical Society
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• v.12 no.4
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• pp.146-149
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• 1968

A new chelate compound, tris(8-bydroxyquinolino)molybdenum(III), [$Mo(C_9H_6ON)_3$], has been prepared by the method of electrolytic reduction of the acidic molybdate solution. Thermal decomposition products of the chelate has been studied by DTA and TGA method. It is concluded that the decomposition product is a yellowish green colored bis(8-hydroxyquinolino)dioxo molybdenum(VI), [$MoO_2(C_9H_6ON)_2$].

• Journal of the Korean Chemical Society
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• v.16 no.2
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• pp.84-92
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• 1972

A mechanism for the ring formation of nickel phthalocyanine (Ni-Pc) has been proposed based on chemical kinetics. The effect of the catalyst on the rate was examined, and ammonium molybdate has been found to be the most effective. The reaction order of the ring formation was determined to be of the 1st order over all, with only the concentration of urea affecting the rate of the ring formation. All the results including thermodynamic parameters support a conclusion that the rate-determining step seems to be the enolization of the urea-catalyst transition complex, followed by fast decomposition of the tautomeric enolized urea into ammonia and isocyanic acid. These intermediates then reacted with the phthalic anhydride to form imino and diimino-phthalimide, which condense to form nickel phthalocyanine in the presence of the nickel cation.

• Applied Chemistry for Engineering
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• v.26 no.6
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• pp.714-718
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• 2015

Both lead molybdate ($PbMoO_4$) and chromium substituted lead molybdate ($PbMo_{1-x}Cr_xO_4$) were successfully synthesized using a conventional hydrothermal method and characterized by XRD, DRS, Raman, SEM and PL. We also investigated the photocatalytic activity of these materials for the decomposition of rhodamine B under UV-visible irradiation. The XRD and Raman results revealed the successful synthesis of well-crystallized $PbMoO_4$ crystals with the diameter of 51-59 nm, regardless of the addition of chromium ion. The DRS spectra of $PbMo_{1-x}Cr_xO_4$ catalysts showed new intensive absorption bands in the visible region. The $PbMoO_4$ catalysts showed the lowest photocatalytic activity and the activity increased with an increase of chromium substitution amounts under visible irradiation. PL peaks appeared at about 540-580 nm for all catalysts and excitonic PL signals were proportional to the photocatalytic activity for the decomposition of rhodamine B.

• Journal of the Korean Ceramic Society
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• v.53 no.4
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• pp.456-462
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• 2016

$NaCaGd(MoO_4)_3:Ho^{3+}/Yb^{3+}$ ternary molybdates were successfully synthesized by microwave sol-gel method for the first time. Well-crystallized particles formed after heat-treatment at $900^{\circ}C$ for 16 h showed a fine and homogeneous morphology with particle sizes of $3-5{\mu}m$. Under excitation at 980 nm, the UC intensities of the doped samples exhibited strong yellow emissions based on the combination of strong emission bands at the 520-nm and 630-nm emission bands in the green and red spectral regions, respectively. The strong 520-nm emission band in the green region corresponds to the $^5S_2/^5F_4{\rightarrow}^5I_8$ transition of $Ho^{3+}$ ions, while the strong 630-nm emission band in the red region appears to be due to the $^5F_5{\rightarrow}^5I_8$ transition of the $Ho^{3+}$ ions. The optimal $Yb^{3+}:Ho^{3+}$ ratio was found at 9:1, as indicated by the composition-dependent quenching effect of $Ho^{3+}$ ions. The pump power dependence of the upconversion emission intensity and the Commission Internationale de L'Eclairage chromaticity coordinates of the phosphors were evaluated in detail.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.40-45
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• 1992

Acidic nucleotidase from Asfiergilius nlger has been partially purified by Sepharose CL-6B gel filtration and DEAE-Sephacel ion exchange chromatography. The optimum pH and temperature for the enzyme reaction with 5'-AMP or 3'-AMP as a substrate were 4.5 and 55%, respectively. However, the optimum temperature became 70% when p-nitrophenyl phosphate was used as a substrate. The enzyme was stable at acidic pH. The enzyme activity was not affected by addition of various nucleotides, nucleosides and inorganic phosphates. Ferric, aluminium, vanadate and molybdate ions inhibited the enzyme activity dramatically. In kinetic studies, $K_m$), values for 3'-AMP, 5'-AMP and p-nitrophenyl phosphate were 1.39 mM, 1.5 mM and 5.77 mM, respectively. The substrate efficiency ($V_{max}/K_m$) shows 3'-AMP is the prefered substrate for the enzyme among tested substrates.