• Animal Bioscience
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• v.35 no.2
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• pp.166-176
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• 2022

Objective: Sperm is particularly susceptible to reactive oxygen species (ROS) stress. Glutathione (GSH) is an endogenous antioxidant that regulates sperm redox homeostasis. However, it is not clear whether boar sperm could utilize cysteine for synthesis GSH to protect sperm quality from ROS damage. Therefore, the present study was undertaken to elucidate the mechanism of how cysteine is involved in protecting boar sperm quality during liquid storage. Methods: Sperm motility, membrane integrity, lipid peroxidation, 4-hydroxyIlonenal (4-HNE) modifications, mitochondrial membrane potential, as well as the levels of ROS, GSH, and, ATP were evaluated. Moreover, the enzymes (GCLC: glutamate cysteine ligase; GSS: glutathione synthetase) that are involved in glutathione synthesis from cysteine precursor were detected by western blotting. Results: Compared to the control, addition of 1.25 mM cysteine to the liquid storage significantly increased boar sperm progressive motility, straight-line velocity, curvilinear velocity, beat-cross frequency, membrane integrity, mitochondrial membrane potential, ATP level, acrosome integrity, activities of superoxide dismutase and catalase, and GSH level, while reducing the ROS level, lipid peroxidation and 4-HNE modifications. It was also observed that the GCLC and GSS were expressed in boar sperm. Interestingly, when we used menadione to induce sperm with ROS stress, the menadione associated damages were observed to be reduced by the cysteine supplementation. Moreover, compared to the cysteine treatment, the γ-glutamylcysteine synthetase (γ-GCS) activity, GSH level, mitochondrial membrane potential, ATP level, membrane integrity and progressive motility in boar sperm were decreased by supplementing with an inhibitor of GSH synthesis, buthionine sulfoximine. Conclusion: These data suggest that boar sperm could biosynthesize the GSH from cysteine in vitro. Therefore, during storage, addition of cysteine improves boar sperm quality via enhancing the GSH synthesis to resist ROS stress.

• Journal of Microbiology and Biotechnology
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• v.4 no.3
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• pp.159-164
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• 1994

Myceliuml growth and spore formation of Streptomyces albidoflavus SMF301 in submerged culture were compared with the metabolism of cysteine. Cysteine added to the culture was metabolized by cysteine desulfhydrase (EC 4.4.1.1.) to produce ammonium ions, hydrogen sulfide, and pyruvate. The redox potential of the culture broth was lowered immediately as the result of the metabolism of cysteine, which caused a lag period of mycelium growth. However enhanced activities of pyruvate dehydrogenase and a-ketoglutarate dehydrogenase were confirmed in the culture containing cysteine, indicating that pyruvate was utilized to support further mycelium growth.

• Bulletin of the Korean Chemical Society
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• v.9 no.3
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• pp.115-117
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• 1988

The addition of L-cysteine without blocking amino and carboxyl groups to${\beta},{\beta}$-dinitrostyrene derivatives(11a-e) were investigated. ${\beta},{\beta}$ -Dinitrostyrene derivatives(11a-e) easily undergo addition reactions with L-cysteine to from s-(2,2-dinitro-1-phenylethyl)-L-cysteine(12a), s-[2,2-dinitro-1-(p-methyl)phenylethyl]-L-cysteine (12b), s-[2,2-dinitro-1-(p-methoxy)phenylethyl]-L-cystein e(12c), s-[2,2-dinitro-1-(p-chloro)phenylethyl]-L-cysteine (12d) and s-[2,2-dinitro-1-(p-nitro)phenylethyl]-L-cysteine( 12a), respectively. The structure of adducts were confirmed by means of spectral data, molecular weight measurement and elemental analysis.

• Textile Coloration and Finishing
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• v.20 no.2
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• pp.9-18
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• 2008

Wool has excellent properties, such as heat retention, absorbency, and elasticity, but it has a disadvantage in washability because the fabric will felt and shrink greatly. Felting causes the interlocking of the fiber surface scales with one another. Therefore, the studies on wool finishing have been focused on shrink proofing. Precedent researches on wool shrink proofing are mostly on eco-friendly method. using enzyme. The purpose of this study is to examine the effect of L-cysteine, EDTA in papain treatment of wool fabrics. The specific contents of study are as follows. Depending on pH, temperature, treatment time, enzyme concentration and L-cysteine, EDTA concentration, weight loss, tensile strength, whiteness, SEM were examined. Each papain treatment conditions depending on L-cysteine, EDTA were optimized from these properties. Papain had very low activation without activators. The optimum conditions of papain treatment were pH 7.5, temperature $75^{\circ}C$, time 30minutes(L-cysteine), 180minutes(EDTA) and papain concentration 5%(o.w.f.). In the use of papain 5%(o.w.f.), the activators optimum concentration was L-cysteine 2%(o.w.f.), EDTA 7%(o.w.f.)

• BMB Reports
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• v.39 no.2
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• pp.150-157
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• 2006

Native grass carp (Ctenopharygodon idellus) growth hormone, has 5 cysteine amino acid residues, forms two disulphide bridges in its mature form. Recombinant grass carp growth hormone, when over-expressed in E. coli, forms inclusion bodies. In vitro oxidative renaturation of guanidine-hydrochloride dissolved recombinant grass carp growth hormone was achieved by sequential dilution and stepwise dialysis at pH 8.5. The redox potential of the refolding cocktail was maintained by glutathione disulphide/glutathione couple. The oxidative refolded protein is heterogeneous, and contains multimers, oligomers and monomers. The presence of non-disulphide-bond-forming cysteine in recombinant grass carp growth hormone enhances intermolecular disulphide bond formation and also non-native intramolecular disulphide bond formation during protein folding. The non-disulphide-bond-forming cysteine was converted to serine by PCR-mediated site-directed mutagenesis. The resulting 4-cysteine grass carp growth hormone has improved in vitro oxidative refolding properties when studied by gel filtration and reverse phase chromatography. The refolded 4-cysteine form has less hydrophobic aggregate and has only one monomeric isoform. Both refolded 4-cysteine and 5-cystiene forms are active in radioreceptor binding assay.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.2
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• pp.201-206
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• 1998

The antibrowning effcts of cysteine, citric acid and ascorbic acid on the browning reaction of enzymatic garlic hydrolyzate were investigated at 37$^{\circ}C$ for 12 days. Cysteine was the most effective antibrowning agent followed by citric acid. The antibrowning effects of cysteine and citric acid were greater as concentrations increased, and the optimal concentration of both cysteine and citric acid as antibrowning agents was 0.3%. Ascorbic acid itself contributed to the browning reaction and showed an accelerating effect as the concentration increased. The addition of 0.1% ascorbic acid as synergist either to 0.3% cysteine or 0.3% citric acid did not enhance significantly the antibrowning effect of cysteine or citric acid. When stored at 3$0^{\circ}C$, 4$0^{\circ}C$ and 5$0^{\circ}C$, the browning reaction was accelerated as the temperature increased, especially at 5$0^{\circ}C$. Even though the effects of citric acid and cysteine as inhibitors on the browning reaction decreased as temperature increased, cysteine was more effective in decreasing browning reaction than citric acid.

• Asian-Australasian Journal of Animal Sciences
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• v.23 no.3
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• pp.318-325
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• 2010

Two experiments were designed to evaluate the effects of the amino acids glycine and cysteine on cryopreservation of ram spermatozoa. After primary evaluation of collected ejaculates, the semen samples were pooled and diluted 1:4 before cooling (experiment 1) and freezing (experiment 2) with Tris-Citrate-Fructose-Yolk (TCFY) extender supplemented with different concentrations of glycine and cysteine (5, 10, 15 and 20 mM). As the control, semen was diluted and frozen in the extender without amino acids. Motility, viability and membrane integrity were assessed as the parameters for semen quality in the first experiment. In the second experiment, motility, progressive motility, viability, membranes and acrosome integrity were evaluated after the freezing-thawing process. The results of the first experiment indicated that the addition of 10 and 15 mM cysteine compared to the control (basic) extender significantly increased (p<0.01) the motility, viability and membrane integrity of spermatozoa after cooling. However, further increasing these amino acids up to 20 mM had a significant negative effect (p<0.05). Our results showed no significant differences (p>0.05) between 5 mM glycine compared to 5 mM cysteine and between 20 mM glycine and 20 mM cysteine. The results of experiment 2 showed that the amino acids significantly improved post-thaw motility, progressive motility, viability, membranes and acrosome integrity of ram spermatozoa. These positive effects were observed at concentrations between 5 to 15 mM of glycine and cysteine, with the best results at 15 mM. Further increasing of amino acid concentrations significantly decreased the post-thaw characteristics of spermatozoa, but the results showed that cysteine was better than glycine and control extenders. The data indicated that addition of glycine or cysteine to the freezing extender can be recommended for cryopreservation of ram spermatozoa. However, further studies are still needed to determine the effect of such addition on fertility in farm animals.

• Korean Journal of Food Science and Technology
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• v.21 no.6
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• pp.800-807
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• 1989

No-time dough process utilizing ascorbic acid as an oxidant was investigated. The farinograph absorption was increased as the amount of L-cysteine increased, while stability and peak time decreased up to 40 and 30 ppm of L-cysteine, respectively. Extensibility of the dough was increased with the increment of L-cysteine, but the ratio of resistance to extensibility was significantly decreased. At the same level of L-cysteine, the addition of ascrobic acid by 1.5 times decreased the farinograph absorption. However, the stability and peak time remained relatively unchanged upon addition of ascrobic acid. Extensibility and resistance of dough were respectively decreased and increased in the presence of both L-cysteine and ascorbic acid. In the range of 30-50 ppm of cysteine, the mixing time decreased and the baking absorption was increased by 1% as the cysteine was increased by 10 ppm. The ascorbic acid had no effects on absorption and mixing time. Bread produced by no·time dough process had no break and shred. The optimum concentrations of L-cysteine and ascorbic acid for no-time dough process were 40 and 100ppm, respectively.

• 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.

• Parasites, Hosts and Diseases
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• v.40 no.2
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• pp.89-92
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• 2002

The cysteine proteases of Paragonimus westermani metacercariae are involved in metacercarial excystment, host immune modulation, and possibly in tissue penetration. In order to clarify the origin of the enzymes, 28 and 27 kDa cysteine proteases in metacercarial excretory-secretory products were purified through the FPLC system using Mono Q column chromatography. The polyclonal antibodies to the enzymes were produced in BALB/c mice. Immunolocalization studies revealed that both cysteine proteases were distributed at the linings of excretory bladder and excretory concretions of the metacercariae. It was suggested that the excretory epithelium of P. westermani undertake the secretory function of metacercarial cysteine proteases, in addition to its role as a route for eliminating waste products.