• Food Science and Biotechnology
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• v.18 no.1
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• pp.234-238
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• 2009

Effects of ginseng on in vivo antioxidant capacities with age were studied in rats. All rats were reared in the conventional system. Ginseng-treated rats were supplied with ginseng water extracts (25 mg/kg/day) continuously from 6 weeks of age to spontaneous death. None of the rats showed any discernible adverse effects of treatment with ginseng-containing water. There was no significant difference in body weight (BW) gains with age between treated and control groups. However, ginseng extracts did cause a decrease in the level of serum low density lipoprotein (LDL)-cholesterol, glucose, and thiobarbituric acid reactive substances (TBARS) in the treated rats. The activities of superoxide dismutase (SOD), catalase, and glutathione peroxidase in liver cytosol decreased with age in the control group. However, these enzyme activities were well maintained in the ginseng-treated rats and, especially, catalase and glutathione peroxidase activities were consistently higher than in control rats. The levels of total sulfhydryl group (T-SH) and glutathione reductase (GR) were unchanged, and glutathione-s-transferase (GST) activity gradually decreased with age in both groups. There were no differences in T-SH, GR, or GST between the control and treatment groups. These results indicate that long-term administration of ginseng retards age-related deterioration in some biochemical parameters such as cholesterol, glucose, and lactate dehydrogenase in serum and it has an enhancing effect on antioxidant capacity in the liver.

• Korean Journal of Veterinary Research
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• v.35 no.3
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• pp.437-445
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• 1995

This experiment was carried out to study the preventive effect of cysteine on the toxicities of captafol to the hematological and serum biochemical values. A single dose of captafol(5mg/kg BW, ip) was given to male Sprague-Dawley rats and its toxicities were evalutated by body weitht changes, autopsy findings, absolute organ weight, and hematological and serum biochemical parameters. The single dose of captafol caused significant decreases in body weitht, and absolute liver weight, as-cites, fibrin clot in abdominal cavity, adhesion of liver lobes significant elevation of number of RBC, hemoglobin concentration and serum AST activity, and decreased of serum phospholipid level. Where as cysteine(over 58mg/kg BW) given immediately after captafol appeared to prevent the ascites, fibrin clot in abdominal cavity and liver lobe adhesion. It also prevented the liver and blood, especially RBC toxicites. The results suggest that cysteine and other compounds containing sulfhydryl groups may protect the subjects from captafol-induced toxicity.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.293-303
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• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be $60^{\circ}C$ and 6.0, respectively.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.5
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• pp.721-733
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• 2019

Objective: The objectives of this study were to investigate the thermal gelation properties and molecular forces of actomyosin extracted from two classes of chicken breast meat qualities (normal and pale, soft and exudative [PSE]-like) during heating process to further improve the understanding of the variations of functional properties between normal and PSE-like chicken breast meat. Methods: Actomyosin was extracted from normal and PSE-like chicken breast meat and the gel strength, water-holding capacity (WHC), protein loss, particle size and distribution, dynamic rheology and protein thermal stability were determined, then turbidity, active sulfhydryl group contents, hydrophobicity and molecular forces during thermal-induced gelling formation were comparatively studied. Results: Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed that protein profiles of actomyosin extracted from normal and PSE-like meat were not significantly different (p>0.05). Compared with normal actomyosin, PSE-like actomyosin had lower gel strength, WHC, particle size, less protein content involved in thermal gelation forming (p<0.05), and reduced onset temperature ($T_o$), thermal transition temperature ($T_d$), storage modulus (G') and loss modulus (G"). The turbidity, reactive sulfhydryl group of PSE-like actomyosin were higher when heated from $40^{\circ}C$ to $60^{\circ}C$. Further heating to $80^{\circ}C$ had lower transition from reactive sulfhydryl group into a disulfide bond and surface hydrophobicity. Molecular forces showed that hydrophobic interaction was the main force for heat-induced gel formation while both ionic and hydrogen bonds were different significantly between normal and PSE-like actomyosin (p<0.05). Conclusion: These changes in chemical groups and inter-molecular bonds affected protein-protein interaction and protein-water interaction and contributed to the inferior thermal gelation properties of PSE-like meat.

• Journal of Microbiology and Biotechnology
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• v.12 no.4
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• pp.669-673
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• 2002

An extracellular limonoate dehydrogenase was purified 10-fold from a cell-free extract of Rhodococcus fascians by ammonium sulfate precipitation, dialysis, and ultrafiltration. This purified dehydrogenase catalyzed the conversion of limonoate to 17-dehydrolimonoate. The enzyme showed optimum activity at pH 8.0 and $40^{\circ}C$, with $K_m$ value of 0.9$\muM$, and requires Zn ions and sulfhydryl groups for catalytic action. The enzyme activity was inhibited by $Hg^{2+}\;and\;NaN_3$ ions. The degradation of limonin (66%) in Kinnow mandarin juice was successfully demonstrated with partially purified limonoate dehydrogenase. With scale-up preparation of limonoate dehydrogenase, a successful debittering operation of fruit juices appears feasible.

• BMB Reports
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• v.30 no.2
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• pp.157-161
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• 1997

The present paper reports characteristics and specificity of the inhibitory action of $N^{\alpha}-tosyl-L-lysine-chloromethyl\;ketone$ (TLCK) and $N^{\alpha}-tosyl-L-phenylalanine-chloromethyl\;ketone$ (TPCK) on the glucose6-phosphate transporter of rat liver microsomes. The TLCK-induced inhibition was pH dependent. The inhibition constants for TPCK were determined by following pseudo-Lst order reaction mechanism. The inhibition was protected by preincubation with excess amount of glucose-6-phosphate. The results proved that (a) TLCK inactivates the microsomal glucose-6-phosphate transporter, (b) the inhibition results from the modification of sulfhydryl groups of the transporter.

• Environmental Analysis Health and Toxicology
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• v.23 no.1
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• pp.33-39
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• 2008

The genotoxicity of mercury compounds have been investigated with a variety of genetic endpoints in prokaryotic and eukaryotic cells. The mercury ions are positively charged and easily form complexes with DNA by binding with negatively charged centers to cause mutagenesis. Further, the mercury ions can react with sulfhydryl (-SH) groups of proteins associated with DNA replication and alter genetic information. Another mechanism by which mercury damages DNA molecule is via its probable involvement of reactive oxygen species (ROS) and induces DNA strand breaks. In order to investigate whether the ROS production was induced by mercury, we performed ROS assay. As the result, the ROS production was significantly increased when it grows dose-dependently and time-dependently. We compared mercury alone-treated group and mercury co-treated with Vitamin C or glutathione group. As the result, the ROS production induced by mercury was decreased by Vitamin C and glutathione. Co-treated with Vitamin C and glutathione group was the most effective to lowering ROS production induced by mercury.

• Food Science and Biotechnology
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• v.16 no.2
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• pp.223-227
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• 2007

Ground garlic inhibited the cross-linking reaction of myosin and incorporation of monodansylcadaverine (MDC) in salted Alaska pollack surimi catalyzed by transglutaminase (TGase). The component responsible for the inhibition was a thermostable, low molecular weight compound. The component also inhibited microbial transglutaminase (MTGase). The inhibition by garlic was reversibly recovered upon addition of 2-mercaptoethanol. The inhibitory component was therefore hypothesized to contain sulfhydryl groups within its structure. Alliin itself did not inhibit the cross-linking reaction. However, the addition of alliin together with garlic increased the inhibition. This result suggested that compounds derived from alliin was responsible for the inhibition of TGase activity.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.297-297
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• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be 60.deg.C and 6.0, respectively.

• Food Science and Biotechnology
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• v.16 no.3
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• pp.404-408
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• 2007

In this study, we investigated the effects by age of long-tenn supplementation of Epimedium koreanum Nakai (EKN)-containing water on the in vivo antioxidant capacities of rats. All rats were reared in a conventional system, and none of the rats showed any signs of aversion to the EKN solution. Neither the mean nor maximum life spans of the rats were extended by long-tenn administration of the solution. The EKN extract caused decreases in the levels of serum thiobarbituric acid reactive substances in the rats. The activities of superoxide dismutase, catalase, and glutathione (GSH) peroxidase within the liver cytosol decreased with age in both the control and EKN-supplemented groups. GSH peroxidase activity, however, was higher at old age in the EKN-supplemented group. The activities of GSH reductase and GSH-S-transferase, and the levels of free-sulfhydryl (SH) and total-SH group gradually decreased with age in both groups. However, there was some tendency for higher levels in the EKN supplemented group at a corresponding age. These results indicate that long-tenn supplementation of EKN water extracts alone does not exhibit discernible adverse effects in rats, and has some enhancing effects on the antioxidant capacities of the blood and liver, but it does not have life-prolonging effects.