• 제목/요약/키워드: trypsin inhibition

검색결과 83건 처리시간 0.023초

Proteinase 활성수용체-2로 유발된 백서족척 부종에 미치는 위릉채의 항염효과 (Anti-inflammatory Effect of Potentillae Chinensis Herba Water Extract on the Proteinase-activated Receptor2-mediated Paw Edema)

  • 임종필;이홍규;전훈;임보라
    • 동의생리병리학회지
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    • 제23권6호
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    • pp.1444-1448
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    • 2009
  • Potentilla chinensis Ser. (Rosaceae) has long been used for a remedy of diarrhea and inflammation in Korea. In this study, the anti-inflammatory effects of the Potentillae chinensis Herba water extract (PCX) was investigated in proteinase-activated receptor-2 (PAR2)-mediated rat paw edema. Paw edema was induced by injection of trypsin or trans-cinnamoyl-LIGRLO-$NH_2$ (tc-$NH_2$) into the hind paw of rats. PCX (10, 50, 100 and 200 mg/kg) was orally administered 1 h before the induction of inflammation. At doses of 50, 100 and 200 mg/kg, PCX showed significant inhibition on both change in paw volume and vascular permeability. PCX (100 mg/kg) significantly inhibited PAR2 agonists-induced myeloperoxidase (MPO) activity in paw tissue. These results indicate that PCX has an anti-inflammatory action in PAR2-mediated paw edema.

어류 알로부터 Protease Inhibitors의 단백질 용해도 차이에 의한 분획 특성 (Fractionation and Characterization of Protease Inhibitors from Fish Eggs Based on Protein Solubility)

  • 김현정;김기현;송상목;김일용;박성환;구은지;이현지;김진수;허민수
    • 한국수산과학회지
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    • 제46권2호
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    • pp.119-128
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    • 2013
  • A protease inhibitor was fractionated from fish eggs using methods based on protein solubility. Fractionation efficiency was evaluated with regard to percent recovery and total inhibitory activity (U). The fractionation of protease inhibitor (PI) from egg extracts of skipjack tuna (ST, Katsuwonus pelamis), yellowfin tuna (YT, Thunnus albacores), and Alaska pollock (AP, Theragra chalcogramma) was performed by precipitation with cold acetone or ammonium sulfate (AS). Fractions exhibiting the strongest inhibitory activity contained 20-40% (v/v) cold acetone or 40-60% saturated AS fractions. AS fractionation was more effective in isolating PI than was precipitation with acetone. The total inhibitory activity and percent recovery of fraction obtained with AS 40-60% toward trypsin and $N{\alpha}$-benzoyl-L-arginine-p-nitroanilide (BAPNA) were 4,976 U and 24.2% for ST, 3,331 U and 38.1% for YT, and 4,750 U and 43.8% for AP, respectively. In comparisons against six commercial proteases, 40-80% AS fractions, made by combining the 40-60% and 60-80% AS fractions from fish egg extract, exhibited the strongest inhibition of trypsin when using a casein substrate. These results suggest that fish eggs act as serine protease inhibitors and may be useful for protease inhibition in foodstuffs.

단백분해효소(蛋白分解酵素)에 의한 대두(大豆) 7S 및 11S 단백질(蛋白質)의 가수분해(加水分解) (Hydrolysis of 7S and 11S Soy Proteins by Commercial Proteases)

  • 강영주;이기춘;박영호
    • 한국식품과학회지
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    • 제20권3호
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    • pp.338-343
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    • 1988
  • 분획(分劃)된 대두(大豆) 7S 및 11S 단백질(蛋白質)의 단백질분해효소(蛋白質分解酵素)(trypsin, alcalase 및 pronase)에 대한 반응성(反應性)을 동력학변수(動力學變數)인 Km 과 Vmax 및 가수분해도(加水分解度)(DH)를 측정(測定)하여 검토(檢討)하였으며 가수분해물의 전기영동분석(電氣泳動分析)을 실시하였다. 효소(酵素)의 대두단백질(大豆蛋白質)에 대한 친화력(親化力)은 대체로 가열처리(加熱處理)된 단백질(蛋白質)은 기질농도(基質濃度) 1.5(w/w) 이하(以下)에서 가수분해(加水分解)에 대하여 기질조해작용(基質阻害作用)을 보였다. 1시간(時間) 가수분해(加水分解)에 따라 alcalase에 의하여 가장 큰 가수분해도(加水分解度)가 얻어졌으며 7S 단백질(蛋白質)에 대하여 60% 및 11S 단백질(蛋白質)에 대하여 80%였다. Trypsin 은 가열처리(加熱處理)되지 않은 단백질(蛋白質)에는 11S 단백질(蛋白質)의 acidic subunit 이외에는 거의 작용(作用)하지 못했으며 alcalase는 특이적으로 2S 단백질(蛋白質)에 변화(變化)를 가져오는 것으로 전기영동분석(電氣泳動分析)에서 나타났다.

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김치에서 분리한 젖산균의 미생물 생육 저해 (Microbial Inhibition of Lactic Strains isolated from Kimchi)

  • 박연희;권정주;조도현;김수일
    • Applied Biological Chemistry
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    • 제26권1호
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    • pp.35-40
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    • 1983
  • 김치에 분리한 젖산균 20주(株)의 Escherichia coli, Staphylococcus aureus 등 5종의 Test organism에 대한 생육저해실험 결과 가장 생육저해능력이 큰 A7 (Pediococcus cerevisiae)와 C4 (Leuconostoc spp.)를 선발하였다. 이 두 균주를 각각 Escherichia coli와 동시에 접종하여 배양한 결과 초기부터 Escherichia coli의 생육을 억제하였으며 약 24시간 후부터는 Escherichia coli의 균수가 급격히 감소하였다. Staphylococcus aureus와 Bacillus cereus에 대하여도 .대체로 비슷한 생육억제작용을 나타내었다. 세가지 Test organism 모두 A7과 배양할 경우 C4의 경우보다 더 큰 death rate constant를 나타내었다 이 혼합 배양액에 catalase를 첨가한 경우 생육저해현상에 영향이 없었으므로 이 두 균주의 생육억계작용은 $H_2O_2$ 생성과 관련이 없는 것으로 나타났다. A7의 배양 여액만을 Escherichia coli 배양액에 첨가한 경우에도 A7균주의 혼합 배양과 동일한 생육저해 현상을 보였으나 여액을 $80^{\circ}C$에서 30분간 열처리후 가하였을 때는 생육저해작용이 거의 나타나지 않을 뿐 아니라 여액에 trypsin 처리한 경우에도 생육저해작용은 크게 억제되었다. 이상의 결과로 A7 균주의 생육저해작용은 단백질류 생육저해물질의 생산에 의한 것이라고 추정할 수 있다.

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Pediococcus pentosaceus K1270에 의한 인공치태 형성억제 효과 (INHIBITION OF BIOFILM FORMATION BY PEDIOCOCCUS PENTOSACEUS K1270 ISOLATED FROM KIMCHI)

  • 최외임;한수지;김신
    • 대한소아치과학회지
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    • 제30권4호
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    • pp.626-636
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    • 2003
  • 치태형성을 억제하는 유산균 K1270을 김치로부터 분리한 후 배양적, 생화학적 특징 및 16S rDNA염기서열 분석에 의해 Pediococcus pentosaceus K1270으로 동정하였다. K1270 균주는 5% 자당이 함유된 배지에서 Streptococcus mutans Ingbritt에 의한 인공치태 형성을 대조군에 비해 94.6 % 억제하였으며, 비수용성 글루캔의 합성을 89.6 % 억제하였다. S. mutans Ingbritt의 증식은 대조군에 비해 100배 정도 억제하였다. K1270균주는 TMB와 peroxidase가 첨가된 MRS 한천배지에서 과산화수소를 생산하였으며, 인공치태 형성에 대한 K1270균주의 억제 효과는 catalase 첨가에 의해 일부 감소되었다. K1270 균주의 배양 상청액을 10% 자당이 함유된 $2{\times}M17$ broth에 동량 가한 경우 인공치태 형성 및 Streptococcus mutans Ingbritt의 증식이 억제되었으며, 이 억제효과는 catalase첨가에 의해 일부 감소되었고, 열처리, 또는 trypsin 처치에 의해 완전히 소실되었다. 따라서, 본 연구에서 분리, 동정된 P. pentosaceus K1270은 과산화 수소와 bacteriocin 유사물질을 분비하여 S. mutans Ingbritt의 증식을 억제함으로써 인공치태 형성을 억제하는 것으로 사료된다.

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Characterization of a New Antidementia $\beta$-Secretase Inhibitory Peptide from Rubus coreanus

  • Lee, Dae-Hyoung;Lee, Dae-Hyung;Lee, Jong-Soo
    • Food Science and Biotechnology
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    • 제17권3호
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    • pp.489-494
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    • 2008
  • In order to develop a potent antidementia $\beta$-secretase inhibitor from phytochemicals, $\beta$-secretase inhibitory activities of extracts from many medicinal plants and herbs were determined. Water extracts from Rubus coreanus showed the highest $\beta$-secretase inhibitory activity of 84.5%. After purification of the $\beta$-secretase inhibitor from R. coreanus using systematic solvent extraction, ultrafiltration, Sephadex G-10 column chromatography, and reverse-phase high performance liquid chromatography (HPLC), a purified $\beta$-secretase inhibitor with $IC_{50}$ inhibitory activity of $6.3{\times}10^3\;ng/mL$ ($1.56{\times}10^{-6}\;M)$ was obtained with a 0.08% solid yield. The molecular mass of the purified $\beta$-secretase inhibitor was estimated to be 576 Da by liquid chromatography-mass spectrometry (LC-MS) and $\beta$-secretase inhibitor also is a new tetrapeptide with the sequence Gly-Trp-Trp-Glu. The purified $\beta$-secretase inhibitory peptide inhibited $\beta$-secretase non-competitively and also show less inhibition on trypsin, however no inhibition on other proteases such as $\alpha$-secretase, chymotrypsin, and elastase.

Characterization of an Amylase-sensitive Bacteriocin DF01 Produced by Lactobacillus brevis DF01 Isolated from Dongchimi, Korean Fermented Vegetable

  • Kang, Tae-Kyu;Kim, Wang-June
    • 한국축산식품학회지
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    • 제30권5호
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    • pp.795-803
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    • 2010
  • A DF01 strain that inhibits tyramine-producing Lactobacillus curvatus KFRI 166 was isolated from Dongchimi, a traditional Korean fermented vegetable, and identified as Lactobacillus brevis by biochemical analysis and reverse transcriptase sequencing of 16S rRNA. The antimicrobial compound produced by L. brevis DF01 was secreted at a maximum level of 640 AU/mL in late exponential phase in MRS broth, and its activity remained constant during stationary phase. The activity of bacteriocin DF01 was totally inactivated by $\alpha$-chymotrypsin, pronase E, proteinase K, trypsin, and $\alpha$-amylase, but not by catalase, which indicates the compound was glycoprotein in nature. The activity was not affected by pH changes ranging from 2 to 12 or heat treatment (60, 80, and $100^{\circ}C$ for 30 min), but was reduced after autoclaving. Bacteriocin DF01 had bacteriolytic activity and a molecular weight of approximately 8.2 kDa, as shown by tricine-SDS-PAGE analysis. Therefore, bacteriocin DF01 can be used in the manufacture of fermented meat products due to its inhibition of tyramine-producing L. curvatus and non-inhibition of L. sake, which is used as a starter culture for meat fermentation.

GBⅠ-Ⅱ 와 관련된 Cyclic Peptide 들의 합성과 단백질 분해 효소에 대한 저해활성 연구 (Synthesis of Cyclic Peticdes Related to GBⅠ-Ⅱand Study of Their Inhibitory Activity for Proteinases)

  • 강신원;허남원
    • 대한화학회지
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    • 제34권3호
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    • pp.288-296
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    • 1990
  • GBⅠ-Ⅱ의 antielastic 고리과 LBI의 antitryptic 고리는 $P_1$ 위치의 아미노산 잔기만 차이가 있으며 나머지 모든 아미노산 잔기는 동일하다. Inhibitor의 $P_1$을 키모트립신에 효과적인 특이성이 있다고 알려진 Tyr 잔기로 치환시킨 cyclic nonapeptide와 저해작용에 필수적으로 생각되는 5개의 아미노산 잔기만으로 선정된 cyclic pentapeptide 유도체를 액상법으로 합성하였다. 이들 펩티드 유도체를 3종의 단백질 분해효소에 작용시켜 그 저해활성을 측정한 결과 cyclic nonapeptide는 키모트립신에는 저해작용이 없었고 의외로 에라스타제와 트립신에 저해활성이 있었다. 또한 cyclic pentapeptide는 키모트립신에만 저해활성이 있었다.

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화피의 충치균과 치주질환균에 대한 항균활성 및 항염효과 (Antibacterial Activity against S. mutans or P. gingivalis and Anti-inflammatory Effect of Betulae Cortex)

  • 임종필
    • 동의생리병리학회지
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    • 제25권4호
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    • pp.635-640
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    • 2011
  • Betulae Cortex of Betula platyphylla Suk. var. japonica Hara (Betulaceae) has long been used for treatment of various inflammation, fever and cough in Eastern Asia. In order to investigate antibacterial activity of the Betulae Cortex against Streptococcus mutans or Porphyromonas gingivalis, MIC (minimal inhibitory concentration) and pH were checked, and for anti-inflammation activity, the experiments about trypsin-induced paw edema, vascular permeability and myeloperoxidase activity in rat's hind-paw tissue, were carried out with various extracts of Betulae Cortex (BCXs) respectively. The BCXs showed significant antibacterial activity, and at the dose of over 50 mg/kg, BCX showed significant inhibition on the paw edema, vascular permeability and myeloperoxidase activity. These results indicate that BCXs have antibacterial activity against oral cariogenic bacteria and anti-inflammatory effect.

어류 알로부터 Protease Inhibitors의 크로마토그래피법에 의한 분획 (Chromatographic Fractionation of Protease Inhibitors from Fish Eggs)

  • 김진수;김기현;김현정;김민지;박성환;이현지;허민수
    • 한국수산과학회지
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    • 제46권4호
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    • pp.351-358
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    • 2013
  • A protease inhibitor from fish eggs was fractionated using chromatographic methods. The fractionation efficiency was evaluated in terms of specific inhibitory activity (SIA, U/mg), purity (fold), total inhibitory activity (TIA, U), and recovery (%). The protease inhibitor (PI) from egg extracts of skipjack tuna (ST Katsuwonus pelamis), yellowfin tuna (YT Thunnus albacares) and Alaska pollock (AP Theragra chalcogramma) was fractionated using Sephadex G-50 gel filtration and DEAE-Sepharose CL-6B anion exchange chromatography based on protein size exclusion and net charge, respectively. Fractions exhibiting strong inhibitory activity were contained in the 30-50 kDa fraction on gel filtration and in the range of 0.4-0.7 M NaCl gradient fraction on anion exchange chromatography. The respective TIA and percent recovery of the fraction obtained with gel filtration toward trypsin and $N{\alpha}$-benzoyl-L-arginine-p-nitroanilide (BAPNA) were 2,758.7 U and 29.6% for ST, 1,005.5 U and 25.6% for YT, and 1,267.5 U and 26.0% for AP. Gel filtration chromatography was more effective at fractionating PI than using ion exchange chromatography. These results suggest that fish eggs act as serine protease inhibitors and might be useful for protease inhibition in foodstuffs.