• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.1
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• pp.160-168
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• 1995

Desmutagenicities against 2-amino-1-methyl-6-phenylimidazo[4, 5-b] pyridine(PhIP) and 2-amino-3, 8-dimethylimidazo[4, 5-f]quinoxaline(MelQx) of tea extracts (steamed green tea, roasted green tea, oolong tea and black tea) were investigated. All the fractions obtained from tea extracts showed strong desmutagenic activity against PhIP and MeIQx toward S. typhimurium TA 98 in the presence of the S-9 mix. The crude catechin fraction exhibited the strongest desmutagenic activity. Among these tea extracts, black tea especially exhibited the strongest desmutagenic activity and the activity was 70.9~91.0% against PhIP and 92.2~98.8% against MelQx at a concentration(0.5~1.0mg/plate) for drinking. The activity of authentic catechins of (-)-EGC, (-)-EGCg, (-)-ECg and (-)-EC were 79.5%, 60.2%, 46.1% and 43.5% against PhIP, and were 52.3%, 11.6%, 8.2% and 22.1% against MelQx by addition of 1.0mg/plate, respectively. The desmutagenic activity was supposedly due to the (-)-EGCg, (-)-EGC and (-)-EC in tea polyphenols, and the browning materials. The desmutagenicity was stronger when mutagens were preincubated with S-9 mix after reaciton with black tea extracts than when preincubated with them after reaction with S-9 mix. The desmutagenicity of tea extracts was rather expressed by reacting directly with mutagens than by deactivating the activated forms of mutagens.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2000.07a
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• pp.94-98
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• 2000

Polycrystalline SBTN ferroelectric thin films were prepared by sol-gel method with various Nb mole ratios on Pt/ $SiO_2$/Si (100) substrates. The films were annealed at different temperatures and characterized in terms of phase and microstructure. Relatively a well saturated hysteresis pattern was obtained at x =0.2 in S $r_{0.8}$B $i_{2.3}$(T $a_{1-x}$ N $b_{x}$)$_2$ $O_{9+}$$\alpha$/ thin films. At an applied voltage of 5V, the dielectric constant ($\varepsilon$$_{r}$) and dissipation factor (tan $\delta$) of typical S $r_{0.8}$B $i_{2.3}$(T $a_{1-x}$ N $b_{x}$)$_2$ $O_{9+}$$\alpha$/ thin film (x=0.2) were about 236.2 and 0.034. Measured remanent polarization (2Pr) and coercive field (Ec) were 4.28C/c $m_2$, and 38.88kv/cm respectively. No fatigue was observed up to 6$\times$10$_{10}$ switching cycles at 5V and the normalized polarization reduced by a factor of only 4%.%. 4%.%. 4%.%.%.%.%.

• Journal of Life Science
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• v.22 no.1
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• pp.98-109
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• 2012

The properties of lactate dehydrogenase (EC 1.1.1.27, LDH) and expression of monocarboxylate transporters (MCTs) 1, 2, and 4 were studied in tissues from Micropterus salmoides. Native-PAGE revealed that the LDH $A_4$ isozyme was predominantly located in skeletal muscle. The LDH $A_4$, $A_2B_2$, and $B_4$ isozymes were detected in heart, liver, eye, and brain tissues, while eye-specific $C_4$ isozyme was detected in eye tissue. In September, strong LDH $B_4$ isozyme activity was detected in heart tissue. High $A_4$ isozyme activity was noted in all other tissues except heart tissue. However, in November, strong $A_4$ isozyme activity was detected in heart tissue. The LDH/CS (Citrate synthase, EC 4.1.3.7) ratio in skeletal muscle and heart tissues indicated that anaerobic metabolism was high in those tissues. Native-PAGE after immunoprecipitation showed that eye-specific $C_4$ isozyme was more similar to the $A_4$ than the $B_4$ isozyme. The LDH $A_4$ isozyme was purified by affinity chromatography. The molecular weight of subunit A was 37,200. The LDH activity in tissues was consistently 11.05~28.32% due to inhibition by 10 mM pyruvate. The $K_m^{PYR}$ of LDH in eye tissue was very low. The optimum pH for LDH in tissues was pH 7.5~8.0. The LDH $A_4$ isozyme was detected in mitochondria of skeletal muscle, whereas the $B_4$ and $A_2B_2$ isozymes were detected in heart tissue mitochondria. Western blot analysis indicated that MCTs 1, 2, and 4 were located in the plasma membrane and mitochondria of skeletal muscle and heart tissues. The sizes of MCTs 1, 2, and 4 in skeletal muscle were 60, 54~38, and 63 kDa, while those in heart tissue were 57, 54~38, and 55.5 kDa, respectively. In conclusion, M. salmoides appears to use anaerobic metabolism predominantly when adapted to a hypoxic environment. In highly activated skeletal muscle and heart tissue, energy production is controlled by inward and outward flows of pyruvate and lactate through MCTs 1, 2, and 4 in the plasma membrane and mitochondria, with effective adjustment by LDH isozymes.

• Journal of Life Science
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• v.20 no.2
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• pp.260-268
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• 2010

The lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes in tissues from Channa argus were purified and characterized by biochemical, immunochemical and kinetic methods. The activity of LDH in skeletal muscle was the highest at 380.4 units and those in heart, eye and brain tissues were 13.4, 3,5 and 5.4 units, respectively. Citrate synthase (EC 4.1.3.7, CS) activity in heart tissue was the highest at 20.7 units. LDH/CS in skeletal muscle, heart, eye and brain tissues were 172.9, 0.6, 0.32 and 0.47. Protein concentration in skeletal muscle tissue was 14.7 mg/g and specific activities of LDH in skeletal muscle, heart, eye and brain tissues were 25.88, 0.79, 0.31 and 1.38 units/mg, respectively. Therefore, skeletal muscle tissue was anaerobic and heart tissue was aerobic. The LDH isozymes in tissues were identified by polyacrylamide gel electrophoresis, immunoprecipitation and Western blot with antiserum against $A_4$, $B_4$, and eye-specific $C_4$. LDH $A_4$, $A_3B$, $A_2B_2$. $AB_3$ and $B_4$ isozymes were detected in every tissue, $C_4$, $AC_3$, $A_2C_2$ and $A_3C$ were detected in eye tissue, and $A_3C$ was found in brain tissue. LDH $A_4$, $A_3B$, $A_2B_2$, $AB_3$, $B_4$, eye-specific $C_4$ isozymes were purified by affinity chromatography and Preparative PAGE Cells. The LDH $A_4$ isozyme was purified in the fraction from elution with $NAD^+$ containing buffer of affinity chromatography. Eye-specific $C_4$ isozyme was eluted right after $A_4$, after which $B_4$ isozyme was eluted with plain buffer. As a result, one part of molecular structures in $A_4$, $B_4$ and eye-specific $C_4$ were similar, but were different from each other in $B_4$ and $C_4$. Therefore the subunit A may be conservative in evolution, and the evolution of subunit B seems to be faster than that of subunit A. The activity of LDH $A_4$, $A_2B_2$, $B_4$, and eye-specific $C_4$ isozymes remained at 39.98, 21.28, 19.67 and 16.87% as a result of the inhibition by 10 mM of pyruvate, so the degree of inhibition was very high. The $Km^{PYR}$ values were 0.17, 0.27 and 0.133 mM in $A_4$, $B_4$ and eye-specific $C_4$ isozymes, respectively. The optimum pH of LDH $A_4$, $B_4$, eye-specific $C_4$, $A_2B_2$, $A_3B$, and $AB_3$ were pH 6.5, pH 8.5, pH 5.5, pH 6.0-6.5, pH 5.0 and pH 7.5. The $A_4$ and heterotetramer isozymes stabilized a broad range of pH. Especially, LDH activities in skeletal muscle tissue were high, resulting in a high degree of muscle activity.LDH metabolism in eye tissue seems to be converted faster from pyruvate to lactate by eye-specific $C_4$ isozyme as eye-specific $C_4$ have the highest affinity for pyruvate, and right after the conversion, oxidation of lactate was induced by $A_4$ isozyme. It was found that expression of Ldh-C, affinity to substrate and reaction time of $C_4$ isozyme were different according to the ecological environmental and feeding capturing patterns.

• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.3
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• pp.412-417
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• 2015

This study was carried out to investigate the effect of steam-drying method on physicochemical properties and antioxidant activities of Alliun hookeri root (AHR). Moisture, crude protein, crude fat, and crude ash contents of raw and steam-dried AHRs were 10.91~14.15%, 11.14~13.49%, 0.83~3.02%, and 7.55~8.98%, respectively. Sulfur contents of steam-dried AHRs were 2.0 and 2.2 times lower than that of raw AHR (0.51%), respectively. pH and total sugar contents of AHRs were reduced by steam-drying, whereas titrate acidity and browning intensity were increased. The L and b values of AHRs in Hunter's value were also reduced, but a value was increased by steam-drying. Among hot water extracts from raw and steam-dried AHRs, four times steam-drying showed the lowest $EC_{50}$ values (0.44, 9.01, and 0.48 mg/mL, respectively) in DPPH radical assay, ABTS radical assay, and reducing power, whereas four times steam-drying had the highest total phenolic content ($34.47{\mu}g/mg$) and browning intensity (2.05 and 0.20 at 280 and 420 nm, respectively). The antioxidant activities of hot water extracts from raw and steam-dried AHRs were closely correlated with their total phenolic contents and browning intensity, showing coefficient of determination ($R^2$) values higher than 0.87. From the results, we suggest that steam-drying method could be used as an effective process for increasing the antioxidant activity of AHR.

• Korean Journal of Animal Reproduction
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• v.21 no.1
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• pp.71-78
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• 1997

This study was conducted to investigate the activation condition of freshly matured bovine IVM oocytes for use as a cytoplasmic recipient in nuclear transfer. Bovine oocytes matured in vitro for 22-24 h were treated with various activation conditions. In Experiment 1 in vitro matured oocytes were treated with electric stimuIus (ES; 2 pulses of 1.25 kV/cm for 70 ${\mu}{\textrm{s}}$ec, each pulse 1 sec apart), ethanol (ET; 7%, 5min) , Ca$^2+$-ionophore(A23187; 10$\mu\textrm{g}$/ml, 5min) and cycloheximide(CH; 10$\mu\textrm{g}$/ml, 6 h). Activation rates were similar in treatments with ES, ET and A23187(48.8~54.3%), however, significantly reduced with CH treatment(15.9%, P