• The Korean Journal of Pharmacology
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• v.26 no.2
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• pp.185-192
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• 1990

The present work was undertaken to investigate the protective effect of diallyl disulfide on the bromobenzene toxicity in mice. It was observed that the aniline hydroxylase and epoxide hydrolase activities were not changed by the treatment of diallyl disulfide for 5 days. But glutathione S-transferase activity was significantly increased. A striking enhancement of serum alanine aminotransferase activity and hepatic lipid peroxide content after bromobenzene administration was markedly decreased by diallyl disulfide pretreatment. These results indicate that the inducing effects of diallyl disulfide on the bromobenzene intermediate detoxifying enzyme such as glutathione S-transferase are believed to be a possible protective mechanism for the bromobenzene toxicity in mice.

• Journal of the East Asian Society of Dietary Life
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• v.3 no.2
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• pp.121-128
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• 1993

This study was intended to clarify the protective mechanism of diallyl disulfide on the carbon tetrachloride-induced hepatotoxicity in mice. It was observed that a powerfully increment of serum alanine aminotransferase activity and hepatic lipid peroxide content after carbon tetrachloride injection were markedly inhibited by the pretreatment of diallyl disulfide (20mg/kg) for 5 days. It was also observed that hepatic aminopyrine demethylase and xanthine ocidase as free radical generating enzymes as well as superoxide dismutase and catalase activities as free frdical scavenging enzymes and hepatic glutathione content were not changed by the pretreatment with diallyl disulfide. But, treatment with diallyl disulfide did signifiantly increase cytosolic glutathione S-transferase activity. However, glutathione S-transferase activity in the presence of diallyl disulfide was not affected in vitro. Therefore, it is concluded that mechanism for the observed preventive effect ofdiallyl disulfide against the carbon tetrachloride-induced hepatotoxicity can be due to the engancement of glutathione S-transferase activity.

• The Korean Journal of Pharmacology
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• v.22 no.2
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• pp.144-150
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• 1986

Glutathione peroxidase might play an important role in the protection of cellular structures against oxidative challange by hydrogen peroxide and several organic hydroperoxides. It is widely accepted that allicin is biological active component of garlic, and allicin is easily degraded to diallyl disulfide and other components. This study was attempted to elucidate the effect of diallyl disulfide on some biological activities. It was observed that the activity of serum transaminase and glutathione level in liver were not changed by the treatment of diallyl disulfide. The liver cytosolic glutathione peroxidase activity was significantly enhanced. Whereas, mitochondrial enzyme activity was slightly increased. In the presence of diallyl disulfide in vitro, $V_{max}$ value of glutathione peroxidase for hydrogen peroxide was increased. On the other hand, Km value was not changed.

• Journal of agricultural medicine and community health
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• v.41 no.2
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• pp.63-74
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• 2016

Objectives: We surveyed the awareness and current status of using fumigant carbon disulfide for exterminate Curculio sikkimensis among chestnut farmers in Chungnam Province to suggest directions for health education and public relations. Methods: We designed questionnaires to evaluate recognition of fumigant carbon disulfide. We conducted a questionnaire survey to assess recognition and recognition level of fumigant carbon disulfide by the study variables. Results: The recognition status for fumigant carbon disulfide was 74.5%, but the recognition level was low (know well 27.5%). The path of recognition was 45.1% and 15.7% for neighbor and rural technology center, respectively. The recognition status for warning label of fumigant carbon disulfide was 52.9%. Recognition for warning label of fumigant carbon disulfide was tended to increase with high educational attainment, bigger owning land area. Recognition on the content of warning label were 29.4%, 27.5%, 21.6%, and 21.6% for inflammability, toxicity, hazard, and explosiveness, respectively. Using personal protection equipment was tended to increase with the high status of awareness on fumigant carbon disulfide. Conclusions: Health education programs for using fumigant carbon disulfide are needed for chestnut farmers. In addition, publicity information activities about prevention and protection of carbon disulfide poisoning are needed for high risk farmers.

• Korean Journal of Veterinary Pathology
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• v.1 no.1
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• pp.13-25
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• 1997

The anticarcinogenic effects of dimethyl disulfide(DMDS, methyl disulfide)and diallyl disulfide(DADA, allyl disulfide) were studied in a 28 weeks rat multi-organ carcinogenesis model. neoplastic and preneoplastic lesions were observed in the liver kidney thyroid gland esophagus duodenum colon, rectum and adrenal gland. Tesults showed that neoplastic lesions in the kidney liver and thyroid gland were inhibited by DADS but those in the liver and colon were enhanced by DMDS when compared to positive control group. incidence of neoplastic lesions in the other organs were not changed by DMDS or DADS exposure. While GST-p positive foci in the liver were increased by DMDS, DADS had no effect. There was no significant histopathological lesion in DMDS or DADS treated group without pretreatment with carcinogens.

• Journal of Life Science
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• v.11 no.5
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• pp.415-422
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• 2001

Many secreted proteins have disulfide bonds that are important for their structure and function. Protein disulfide isomerase (PDI, EC 5.3.1.4.), an enzyme that catalyzes the formation and rearrangement of thiol/disulfide exchange reactions, is a resident of the endoplasmic reticulum (ER). The subcellular localization and its function as catalyst of disulfide bond formation in the biosynthesis of secretory and cell membrane proteins suggest that PDI plays a key role in the secretory pathway. We have isolated a cDNA encoding protein disulfide isomerase from Bombyx mori(bPDI). It has been characterized under ER stress conditions (dominantly induced by calcium ionophore A23187, tunicamycin and DTT), which is known to cause an accumulation of unfolded proteins in the ER. Furthermore, It has also been examined for tissue distribution(pronounced at the fat body), hormonal regulation (juvenile hormone, insulin and juvenile +transferrin; however, it is not effected by transferrin alone), and the effect of exogenous bacteria (peak at 16 h after infection) on the bPDI mRNA expression. The results suggest that bPDI is a member of the ER stress protein group, and it may play an important role in exogenous bacterial infection in fat body, and that homones regulate its expression.

• Archives of Pharmacal Research
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• v.9 no.4
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• pp.205-209
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• 1986

Glutathione s-transferase in thought to play a key role in initiating the detoxication of potential alkylating agents, including pharmacologically active compounds. It is widely accepted that garlic contained allin which is converted to allicin by allinase. Allicin is easily degraded to diallyl disulfide and other components. This report attempted to observe the effect of diallyl disulfide on some biological activities. It was observed that the activity of serum transaminase was not changed by the treatment of diallyl disulfide. The liver cytosolic glutathione s-transferase was significantly increased. where as the microsomal glutathione s-transferase was not increased.

• Textile Coloration and Finishing
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• v.1 no.1
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• pp.1-6
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• 1989

The reaction of silk with a disulfide-containing crosslinking agent, i.e. bis($\beta$-isocyanatoethyl)disulfide(BIED), was studied in an attempt to obtain disulfide-crosslinked silk. The setting properties of disulfide-crosslinked silk fibers were studied. The permanent set values of single fibers were evaluated after the set fibers were relaxed in boiling water. When single fibers were set in boiling water or in boiling alkaline solution, the permanent set values of BIED-treated silk fibers were less than those of untreated silk fibers. When the fibers were treated with 2% thioglycolic acid solution at $60^\circ{C}$ followed by oxidation, settability of BIED-treated silk was better than that of untreated silk. The rearrangement of secondary bonds faciliated by cleavage of crosslinks as well as the rearrangement of crosslinks itself seems to be an important role in the set stability.

• Bulletin of the Korean Chemical Society
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• v.26 no.4
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• pp.553-557
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• 2005

The formation of striped phases of unsymmetric hexyl octadecyl disulfide ($CH_3(CH_2)_5SS(CH_2)_{17}CH_3$, HOD) and 1-hydroxyundecyl octadecyl disulfide ($CH_3(CH_2)_{17}SS(CH_2)_{11}$OH, HUOD) on Au(111) and graphite has been investigated by scanning tunneling microscopy (STM) to understand the self-assembly processes of dialkyl disulfides. STM imaging clearly shows the formation of striped phases having corrugation periodicities that are nearly consistent with the molecular length of alkanethiolate moieties formed after the S-S bond cleavage of dialkyl disulfide on a gold surface. On the other hand, self-assembled monolayers (SAMs) of dialkyl disulfides on a graphite surface displayed long-range, well-ordered monolayers with one striped pattern that shows periodicity as a function of molecular length via nondissociative adsorption. From a nonoscopic viewpoint, we have clearly demonstrated that dialkyl disulfide SAMs on gold form via S-S bond cleavage of disulfide.

• Mass Spectrometry Letters
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• v.1 no.1
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• pp.5-8
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• 2010

In the present study, collisionally-activated dissociation (CAD) experiments were performed under low energy collision conditions in six peptides containing a disulfide bond. Fragments produced as a result of the cleavage of a disulfide bond were obtained after CAD in four peptides (bactenecin, TGF-$\alpha$, cortistantin, and linearly linked peptide, Scheme 1) with basic amino acid residues. In contrast, the CAD analysis of two peptides with no basic residue (oxytocin and tocinoic acid) rarely produced fragments indicative of cleavage of a disulfide bond. These results are consistent with the mobile proton model suggested by the McLuckey and O'air groups (ref. 22 and 23); nonmobile protons sequestered at basic amino acid residues appear to promote the cleavage of disulfide bonds.