• Food Science of Animal Resources
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• v.39 no.4
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• pp.576-584
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• 2019

This study was performed to evaluate the physicochemical properties of myofibrillar protein (MP) gels containing pork skin gelatin at different salt concentrations. MP gels were prepared to the different salt levels (0.15, 0.30, and 0.45 M) with or without 1.0% of pork skin gelatin. Cooking yield (CY), gel strength, shear stress were measured to determine the physical properties, and SDS-polyacrylamide gel electrophoresis, scanning electron microscopy, fourier transform infrared spectroscopy, sulfhydryl group and protein surface hydrophobicity was performed to figure out the structural changes among the proteins. The addition of gelatin into MP increased CYs and shear stress. MP at 0.45 M salt level had the highest CY and shear stress, as compared to MPs at lower salt concentrations. As the salt concentration of MP gels increased, the microstructure became the compact and wet structures, and decreased the amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$. MP with gelatin showed a decreased amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$ compared to MP without gelatin. The addition of gelatin to MP did not affect the sulfhydryl group, but the sulfhydryl group decreased as increased salt levels. MP mixtures containing gelatin showed a higher hydrophobicity value than those without gelatin, regardless of salt concentration. Based on these results, the addition of gelatin increased viscosity of raw meat batter and CY of MP gels for the application to low salt meat products.

• Journal of Oriental Physiology
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• v.14 no.2 s.20
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• pp.1-9
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• 1999

Ethanol induces compoundhemorrhagic gastric lesions and causes a dose-dependent decrease in the concentration of endogenous nonprotein sulfhydryls in rat gastric mucosa. Sulfhydryl-containing drugs protect rats from ethanol - induced gastric lesions. Based on this findings, we investigated the involvement of sulfhydryl compounds in the antioxidant effects of Puerariae radix, a traditional herbal medicine, against ethanol - induced gastric lesions in the absence and presence of iodoacetamide(IDA. sulfhydryl blocking agent) in rats. respectively. Because of the known role of sulfhydryls in gastric cytoprotection, its role in gastric antioxidation was of intrest. In vitro, Puerariae radix extract(PRE) reduced linoleic acid autooxidation and exert DPPH radical scavenging effect. In vivo. PRE increased antioxidants(SOD, catalase. GSH) and reduced lipid peroxide level in ethanol-induced gastric mucosal lesions. But treatment with PRE plus IDA significantly inhibit the antioxidant effects such as SOD and GSH but did not affect catalase levels. These results suggest that Puerariae radix may play roles in the gastric cytoprotection through antioxidant effects and increase of SOD activity and GSH level are dependent of endogenous sulfhydryls.

• Microbiology and Biotechnology Letters
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• v.21 no.1
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• pp.30-35
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• 1993

Clp is a relatively abundant ATP-dependent protease found in E. coli. Its specific activity was proportional to the concentration of the limiting amount of Clp A and an excess amount of Clp P, and vice versa. Clp A has an intrinsic ATPase activity that is stimulated by casein, and contains a second site for binding A TP, in addition to the ATPase site. The modification of sulfhydryl groups in Clp A with reagents which have bulky groups such as N-phenylmaleimide led to nullifying both ATPase and protease activity. The same sites were modified by sulfhydryl reagents. It seems that the sulfhydryl groups of Clp A are not directly involved in catalysis. Since non-hydrolyzable analogs of ATP do not activate Clp, ATP hydrolysis may be essential for the proteolytic activity of Clp protease. Clp A and Clp P did not associate in the absence of nucleotide. The results suggest that the activity of the proteolytic component, Clp P, is regulated by the A TP-dependent cycling of Clp A between the activator form and the non-activator form.

• Journal of Acupuncture Research
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• v.19 no.5
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• pp.209-218
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• 2002

Objective : This study was undertaken to examine whether Carthami Semen aquacupuncture (CSA) exerts protective effect against Hg-induced cell injury in rabbit liver. Methods : The cell injury was evaluated by ALT activity and lipid peroxidation was estimated by measuring malondialdehyde (MDA). Results : Hg caused an increase of ALT activity and lipid peroxidation in a dose-dependent-manner over concentrations of 0.1-1 mM, which were prevented by addition of 0.005% CSA. The protective effect of CSA was dose-dependent in concentration range of 0.001 to 0.01%. The increase of ALT activity and lipid peroxidation induced by 0.5 mM Hg were almost completely decreased by addition of 0.01% CSA. When the liver tissues were exposed to 0.5 mM Hg, GSH content was decreased, which was significantly restored by 0.01% CSA. 0.5 mM Hg caused decrease in the amount of total and nonprotein sulfhydryl groups, and 0.01% CSA prevented Hg-induced reduction of nonprotein sulfhydryl group but not protein sulfhydryl group. Conclusions : These results suggest that CSA exerts protective effect against Hg-induced cell injury by antioxidant action resulting from enhancement of nonprotein sulfhydryl group content including GSH in liver.

• Journal of Radiation Protection and Research
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• v.31 no.2
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• pp.65-68
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• 2006

In this study, the extent of plasmid DNA damage was observed according to concentration of BSH(Boron Sulfhydryl Hydride) and irradiation doses of neutron and ${\gamma}$-ray. The plasmid used was both pBR 322 (2870 bp) and ${\Phi}X174$ RF(5386 bp) DNA. Plasmid DNA damage by irradiation in the presence of BSH was analyzed by agarose gel electrophoresis. In the neutron experiment, DNA damage of both plasmid DNAs was increased according to increasing the concentration of BSH and neutron doses. But in the ${\gamma}$-ray experiment, there appeared no dose dependency as compared to the neutron experiment. The extent of the plasmid DNA damage in the presence of BSH was somewhat different according to irradiation by neutron or ${\gamma}$-ray.

• Microbiology and Biotechnology Letters
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• v.19 no.3
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• pp.308-312
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• 1991

The delta-endotoxin from B. thuringiensis subsp. damstadienszs 73E10-2 was resistant to high concentration of salt (4M NaBr), organic solvents (50% acetone), denaturants (4 M urea), and neutral detergents (10% triton X-100). In contrast, the toxin was inactivated by treating with charged detergents as well as guanidine hydrochloride or carbon tetra-chloride. The delta-endotoxin is not a sulfhydryl activated toxin, but modification of the lysine side chains eliminated toxicity against mosquito larvae.

• The Korean Journal of Physiology
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• v.10 no.2
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• pp.1-10
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• 1976

The action of acetylcholine on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of acetylcholine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is inhibited by acetylcholine. 2. The ratio of inhibition of NaK ATPase by acetylcholine is decreased by raising the potassium concentration, and is increased by raising the sodium concentration. 3. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts. The ratio of inhibition of the enzyme by acetylcholine is increased by raising the calcium concentration. 4. The inhibitory action of acetylcholine on the NaK ATPase activity was not related to the sulfhydryl group of cysteine, the hydroxyl group of threonine, or the carboxyl group of aspartic acid. 5. The inhibitory action of acetylcholine on the ATPase activity is due to amino group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• v.8 no.1
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• pp.67-76
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• 1974

The effect of saponin on the sodium plus potassium activated ATPase activity was studied in the rabbit red cell ghosts and the experiments were also designed to determine the mechanism of action of saponin on the APTase activity. The following results were observed. 1. The ATPase activity of rabbit red cell ghosts is inhibited by low concentration of saponin but increased by high concentration. The activating effect of saponin on the $Na^{+}-K^{+}-ATPase$ activity is inhibited by ouabain but the stimulation of the $Mg^{++}-ATPase$ by high concentration of saponin is not inhibited by ouabain. 2. The activity ratio of $Na^{+}-K^{+}-ATPase$ by high concentration of saponin is decreased by raising the potassium concentration, and is increased by raising the sodium concentration. 3. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts. The activity ratio of the enzyme by saponin is decreased by raising the calcium concertration 4. The action on the ATPase activity was not related to the amino group of lysine, the hydroxyl group of threonine, the imidazole group of histidine, or the carboxyl group of aspartic acid. 5. The action of saponin on the ATPase activity is due to sulfhydryl group of the enzyme of $Na^{+}-K^{+}-ATPase$.

• The Korean Journal of Physiology
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• v.12 no.1_2
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• pp.15-23
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• 1978

The action of ascorbic acid on the sodium Plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action if ascorbic acid on the ATPase activity The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by ascorbic acid and the concentration of ascorbic acid for maximal activity is about 8 mM. 2. The activating effect of ascorbic acid on the ATPase activaty, with a given concentration of sodium in the medium, is increased by raisins the potassium concentration but activity ratio is decreased. 3. The activating effect of ascorbic acid on the ATPase activity, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 4. The action of ascorbic acid on the ATPase activity is stimulated by calcium ions and activity ratio is increased by raising the calcium concentration. 5. The activating effect of ascorbic acid on the ATPase activity was not related to the sulfhydryl group of cysteine or the hydroxyl group of threonine. 6. The activating effect of ascorbic acid on the ATPase activity is due to amino group and carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• v.10 no.1
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• pp.15-24
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• 1976

The action of aconite on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of aconite on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by aconite, and the concentration of aconite for maximal activity is about 80 mg%. The pH optimum for the aconite sensitive component is 8.0. 2. The activating effect of aconite on the ATPase, with a given concentration of sodium in the medium, is increased by raising the potassium concentration but activity ratio is decreased. 3. The activating effect of aconite on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 4. The action of aconite on the ATPase activity is inhibited by calcium ions and the effect of inhibition is increased by small amounts of calcium but decreased by larger amounts. 5. The activating effect of aconite on the ATPase was not related to the sulfhydryl group of cysteine, the amino group of lysine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The action of aconite on the ATPase activity is due to carboxyl group of the enzyme of NaK ATPase.