• 제목/요약/키워드: Disulfide

검색결과 724건 처리시간 0.032초

돌산 갓 김치 숙성 중 매운맛 성분의 변화 (Changes in Pungent Components of Dolsan Leaf Mustard Kimchi during Fermentation)

  • 전순실;최옥자;조영숙;박석규;박정로
    • 한국식품영양과학회지
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    • 제24권1호
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    • pp.54-59
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    • 1995
  • 돌산 갓(Brassica juncea) 김치 개발의 일환으로 갓 김치 숙성 중의 휘발성 성분을 분리, 동정하였으며, 매운 맛 성분인 glucosinolate의 함량변화를 분석하였다. 돌산 갓 김치의 숙성 중의 주요 휘발성 성분은 3-isothi-ocyanate-1-propene(Allyl isothiocyanate)이었으며, 그 외 di-2-propenyl disulfide, 1-methoxy1-2-butanol, 4-isothiocyanate-1-butene, di-2-propenyl disulfide 그리고 dimethyl-trisulfied 등 이었다. 갓 김치가 발효됨에 따라 AITC와 4-isothiocyanate-1-butene은 점차 감소하였지만, dimethyl trisulfide는 발효 저장 중에 다소 증가 하였다. Di-2-propenyl disulfide는 5일 까지 감소되었다가 10일 이후에는 다소 증가하였다. 갓 김치 숙성 중의 매운맛 성분인 총 glucosinolate 함량은 3일 까지 증가하다가, 그 이후는 감소하는 경향을 보였다.

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Role of Protein Disulfide Isomerase in Molecular Fate of Thyroglobulin and its Regulation by Endogenous Oxidants and Reductants

  • Liu, Xi-Wen;Sok, Dai-Eun
    • Archives of Pharmacal Research
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    • 제25권4호
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    • pp.485-492
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    • 2002
  • The molecular fate of thyroglobulin (Tg) is controlled by oligomerization, a means of storing Tg at high concentrations, and deoligomerization. The oligomerization of bovine Tg are intermolecular reactions that occur through oxidative processes, such as disulfide and dityrosine formation, as well as isopeptide formation; disulfide formation is primarily responsible for Tg oligomerization. Here, the protein disulfide isomerase (PDI) and/or peroxidase-induced oligomerization of unfolded thyroglobulins, which were prepared by treating bovine Tg with heat, urea or thiol/urea, was investigated using SDS-PAGE analyses. In addition, the enzymatic oligomerization was compared with non-enzymatic oligomerization. The thermally-induced oilgomerization of Tg, dependent on glutathione redox state, was affected by the ionic strength or the presence of a surfactant. Meanwhile, PDI-catalyzed oligomerization, time and pH-dependent, was the most remarkable with unfolded/reduced Tg, which was prepared from a treatment with urea/DTT, while the thermally-unfolded Tg was less sensitive. Similarly, the oligomerization of unfolded/reduced Tg was also mediated by peroxidase. However, PDI showed no remarkable effect on the peroxidase-mediated oligomerization of either the unfolded or unfolded/reduced Tg. Additionally, the reductive deoligomerization of oligomeric Tg was exerted by PDI in an excessively reducing state. Based on these results, it is proposed that PDI catalyzes the oligomerization of Tg through the disulfide linkage and its deoligomerization in the molecular fate, and this process may require a specific molecular form of Tg, optimally unfolded/reduced, in a proper redox state.

김치재료의 주요한 냄새성분과 김치숙성중의 냄새성분 및 관능적특성의 변화 (Major Odor Components of Raw Kimchi Materials and Changes in Odor Components and Sensory Properties of Kimchi During Ripening)

  • 정혜승;고영태
    • 한국식생활문화학회지
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    • 제25권5호
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    • pp.607-614
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    • 2010
  • Changes in major volatile odor components (VOC) and sensory properties of kimchi during ripening for 4 days were investigated, and major VOCs of the raw materials of kimchi were also analyzed. Seven of eight major VOCs of kimchi originated mainly from garlic, while one originated from ginger. During 4 days of kimchi ripening, the amount of ethanol, which was substantially higher than that of other VOCs, increased continuously but decreased slightly on the fourth day. The amount of diallyl disulfide decreased during ripening, while that of allyl mercaptan decreased on the first day and increased slightly thereafter. The amount of methyl allyl sulfide, diallyl sulfide, and methyl trisulfide increased continuously during ripening, while that of dimethyl disulfide and methyl propyl disulfide increased until the second day and decreased thereafter. Scores of overall acceptability, taste, and odor for kimchi ripened for 2 days were significantly higher than those of other samples (p<0.05). The correlation between scores of overall acceptability and the amount of dimethyl disulfide or methyl propyl disulfide was higher than that of other VOCs.

천연 단백질섬유의 세트성 증진 (Improvement of the Setting Properties of Natural Protein Fibers)

  • Jang, Byung-Ho;Nam, Sung-Woo
    • 한국염색가공학회지
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    • 제2권2호
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    • pp.14-19
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    • 1990
  • The setting behavior of disulfide-enriched wool and disulfide-crosslinked silk obtained by treatment with a disulfide-containing crosslinking agent, bis $(\beta-isocyanatoethyl)$ dissulfide was compared with that of untreated wool and silk under the absence and the presence of a reducing agent. Rearrangment of secondary bonds facilitated by cleavage of crosslinks as well as rearrangement of crosslinks itself seems to play an important role in the set stability.

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3-멀?토-4H-피롤로피리딘의 합성 (Synthesis of 3-mercapto-4H-pyrrolopyridine)

  • 마은숙
    • 약학회지
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    • 제46권6호
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    • pp.369-374
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    • 2002
  • Dilithiation of 4-(pivaloylamino)pyridine (5) followed by reaction with tetraisopropylthiuram disulfide(TITD) gave rise to 3-(diisopropyldithiocarbamato)-4-(pivaloylamino)pyridine (6). 3-Mercapto-4H-pyrrolopyridine(2) was synthesized from compound 6 by two methods. The first method was that compound 6 was treated with 5M-HCl to form 2-t-butylthiazolo[5,4-c]pyridine (7) and hydrolysed in refluxing 10% NaOH and solid NaOH to prepare bis(4-amino-3-pyridyl)disulfide (8). And compound 8 was reacted with 2,5-dimethoxytetrahydrofuran and NaBH$_4$ to afford compound 2. The second method was that compound 6 was hydrolysed with 10% NaOH and followed to react with 2,5-dimethoxytetrahydrofuran to form compound 11. And then compound 11 was treated with 20% ethanolic KOH solution to synthesize compound 2.

Emerging roles of protein disulfide isomerase in cancer

  • Lee, Eunyoug;Lee, Do Hee
    • BMB Reports
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    • 제50권8호
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    • pp.401-410
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    • 2017
  • The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine-based redox reactions and assist the quality control of client proteins. Recent structural and functional studies have demonstrated that PDI members not only play an essential role in the proteostasis in the ER but also exert diverse effects in numerous human disorders including cancer and neurodegenerative diseases. Increasing evidence suggests that PDI is actively involved in the proliferation, survival, and metastasis of several types of cancer cells. Although the molecular mechanism by which PDI contributes to tumorigenesis and metastasis remains to be understood, PDI is now emerging as a new therapeutic target for cancer treatment. In fact, several attempts have been made to develop PDI inhibitors as anti-cancer drugs. In this review, we discuss the properties and diverse functions of human PDI proteins and focus on recent findings regarding their roles in the state of diseases including cancer and neurodegeneration.

HL-60 세포에서 Diallyl Disulfide의 Daunorubicin 유발 Apoptosis 항진효과 (Diallyl Disulfide Enhances Daunorubicin-Induced Apoptosis of HL-60 Cells)

  • 구본선;양정예;손희숙;권강범;지은정
    • Journal of Nutrition and Health
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    • 제36권8호
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    • pp.828-833
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    • 2003
  • Dially disulfide (DADS), a component of garlic (Allium sativum), has been known to exert potent chemopreventive activity against various cancers. In this study, the synergistic effect of DADS and daunorubicin on the cytotoxicity of HL-60 cells, a human leukemia cell line, was investigated. DADS at 25 M greatly potentiated daunorubicin-induced cell death, decreasing cell viabilityto50%ofthe control. Daunorubicin-induced apoptosis was accompanied by the activation of caspase-3, the degradation of poly-(ADP-ribose) polymerase (PARP) and D4-GDI, and DNA fragmentation, which were blocked by pre-treatment with acetyl-Asp-Glu-Val-Asp- dialdehyde (Ac-DEVD-CHO). Treatment that combined 25 M DADS and 100 nM daunorubicin caused a similar degree of caspase-3 activation, PARP and D4-GDI degradation, and DNA fragmentation to that caused by treatment with 250 nM daunorubicin alone. These results indicate that combined therapy using daunorubicin with DADS, a component of food, and garlic can effectively decrease the therapeutic dose of daunorubicin, preventing the severe side effects of daunorubicin.

Activity of Human Dihydrolipoamide Dehydrogenase Is Reduced by Mutation at Threonine-44 of FAD-binding Region to Valine

  • Kim, Hak-Jung
    • BMB Reports
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    • 제35권4호
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    • pp.437-441
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    • 2002
  • Dihydrolipoamide dehydrogenase (E3) is a member of the pyridine nucleotide-disulfide oxidoreductase family. Thr residues are highly conserved. They are at the active site disulfide-bond regions of most E3s and other oxidoreductases,. The crystal structure of Azotobacter vinelandii E3 suggests that the hydroxyl group of Thr that are involved in the FAD binding interact with the adenosine phosphate of FAD. However, several prokaryotic E3s have Val instead of Thr. To investigate the meaning and importance of the Thr conservation in many E3s, the corresponding residue, Thr-44, in human E3 was substituted to Val by site-directed mutagenesis. The mutant’s E3 activity showed about a 2.2-fold decrease. Its UV-visible and fluorescence spectra indicated that the mutant might have a slightly different microenvironment at the FAD-binding region.

Coexpression of Protein Disulfide Isomerase (PDI) Enhances Production of Kringle Fragment of Human Apolipoprotein(a) in Recombinant Saccharomyces cerevisiae

  • Cha Kwang-Hyun;Kim Myoung-Dong;Lee Tae-Hee;Lim Hyung-Kweon;Jung Kyung-Hwan;Seo Jin-Ho
    • Journal of Microbiology and Biotechnology
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    • 제16권2호
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    • pp.308-311
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    • 2006
  • In an attempt to increase production of LK8, an 86-amino-acid kringle fragment of human apolipoprotein(a) with three disulfide linkages, protein disulfide isomerase (PDI) was coexpressed in recombinant Saccharomyces cerevisiae harboring the LK8 gene in the chromosome. Whereas overexpression of the LK8 gene without coexpressing PDI was detrimental to both host cell growth and LK8 production, coexpression of PDI increased the LK8 production level by 2.5-fold in batch cultivation and 5.0-fold in fed-batch cultivation compared with the control strain carrying only the genomic PDI gene.

Recycling Natural Rubber Vulcanizates through Mechanochemical Devulcanization

  • Jang G. K.;Das C. K.
    • Macromolecular Research
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    • 제13권1호
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    • pp.30-38
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    • 2005
  • Sulfur-cured gum natural rubber vulcanizates were devulcanized using two different concentrations of diallyl disulfide. The devulcanization process was performed at $110^{\circ}C$ min in an open two-roll cracker-cum-mixing mill. Natural rubber vulcanizates having various sulfur/accelerator ratios were used to study the cleavage of monosulfide, disulfide, and polysulfide bonds. The properties of devulcanized natural rubber increased upon increasing the disulfide concentration and the mechanical properties of the revulcanized natural rubber increased upon decreasing the sulfur content in the original rubber vulcanizates. The scorch time and the maximum state of cure both increased when the ground vulcanizates were treated with higher amounts of disulfide. TGA and DMA were conducted to study the effects of the devulcanization on the thermal stability and the $T_g$ behavior of the vulcanizates. SEM analysis was conducted to study how the failure mechanism was affected by the devulcanization process. It was possible to recover $70-80\%$ of the original gum rubber properties by using this process. From IR spectroscopic analysis, we observed that the oxidation of the main chains did not occur during high-temperature milling.