• Korean Journal of Food Science and Technology
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• v.14 no.3
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• pp.197-202
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• 1982

Kinetic study for the thermal degradation of ginsenosides in ginseng extract was conducted. The results indicate that the thermal degradation followed first order kinetics and rate constants varied substantially depending on the types of ginsenosides and heat treatment temperatures. Activation energy calculated by Arrhenius plots ranged from 16.80 kcal/mole to 30.10 kcal/mole and $Q_{10}$ values ranged from 2.01 to 3.49. Correlation coefficients between the change of ginsenoside contents by thermal degradation and heat treatment temperature were $0.995{\sim}0.999$. The dependence on temperatures of the decomposition rate constant of total ginsenoside can be expressed as $k=4.574{\times}10^8$ exp(8898.8/T).

• Journal of the Korean Chemical Society
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• v.36 no.4
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• pp.511-516
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• 1992

The x-values of the nonstoichiometric compound YbO$_x$ have been measured in a temperature range of 600 to 1150$^{\circ}C$ under oxygen partial pressure of 1.00 ${\times}$ 10$^{-2}$ atm∼atmospheric air pressure. The values are varied between 1.55453 and 1.60794 in the conditions. The enthalpy of the formation for x' in YbO$_{1.5＋x'}$(${\Delta}$H$_f$) was 1.55, 1.18, and 1.05 kJ/mol under the above conditions, respectively. The electrical conductivities of the oxides or ${\sigma}$ have been measured in the temperature range from 600 to 1100$^{\circ}C$ under oxygen partial pressure of 1.00 ${\times}$ 10$^{-5}$ ∼ 2.00 ${\times}$ 10$^{-1}$ atm. They varied from 10$^{-9}$ to 10$^{-5}$ ohm$^{-1}$ cm$^{-1}$ within the semiconductor range. The Arrhenius plots of the electrical conductivities show a linearity and the activation energy for the conduction was about 1.7eV. The oxygen partial pressure dependence of the conductivity or 1/n value increases with the pressure. The nonstoichiometric conduction mechanism of the oxide was discussed in terms of the x values, ${\sigma}$ values, and the thermodynamic data.

• The Korean Journal of Physiology
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• v.20 no.2
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• pp.257-270
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• 1986

It has been reported that the luteal function may be regulated by the intracellular calcium in luteal cells (Higuchi et al, 1976; Dorflinger et at, 1984; Gore and Behrman, 1984) which is adjusted partially by $Ca^{++}-ATPase$ activities in luteal cell membranes (Verma and Pennistion, 1981). However, the physicochemical and kinetic properties of $Ca^{++}-ATPase$ in luteal membranes were not fully characterized. This study was, therefore, undertaken to partially characterize the physicochemical and kinetic properties of $Ca^{++}-ATPase$ system in luteal membranes and microsomal fractions, known as an one of the major $Ca^{++}$ storge sites (Moore and Pastan, 1978), from the highly luteinized ovary Highly luteinized ovaries were obtained from PMSG-hCG injected immautre female rats. Light membrane and heavy membrane fractions and microsomal fractions were prepared by the differential and discontinuous sucrose density gradient centrifugation method desribed by Bramley and Ryan (1980). Light membrane and heavy membrane fractions and microsomal fractions from highly luteinized ovaries are composed of the two different kinds of $Ca^{++}-ATPase$ system. One is the high affinity $Ca^{++}-ATPase$ which is activated in low $Ca^{++}$ concentration (Km, 10-30 nM), the other is low affinity $Ca^{++}-ATPase$ activated in higher $Ca^{++}$ concentration $(K_{1/2},\;40\;{\mu}M)$. At certain $Ca^{++}$ concentrations, activities of high and low affinity $Ca^{++}-ATPase$ are the highest in light membrane fractions and are the lowest in microsomal fractions. It appeares that high affinity $Ca^{++}-ATPase$ system have 2 binding sites for ATP (Hill's coefficient; around 2 in all membrane fractions measured) and the positive cooperativity of ATP bindings obviously existed in each membrane fractions. The optimum pH for high affinity $Ca^{++}-ATPase$ activation is around S in all membrane fractions measured. The lipid phase transition temperature measured by Arrhenius plots of high affinity $Ca^{++}-ATPase$ activity is around $25^{\circ}C$. The activation energies of high affinity $Ca^{++}-ATPase$ below the transition temperature are similar in each membrane fractions, but at the above transition temperature, it is the hightest in heavy membrane fractions and the lowest in microsomal fractions. According to the above results, it is suggested that intracellular $Ca^{++}$ level, which may regulate the luteal function, may be adjusted primarily by the high affinity $Ca^{++}-ATPase$ system activated in intracellular $Ca^{++}$ concentration range $(below\;0.1\;{\mu}M)$.