• Title, Summary, Keyword: fibrinolytic activity

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Studies on the Fibrinolytic Effect of Germinated Grain Seeds

  • Kwon, Su-Jung;Lee, Jang-Won;Park, Min-Hee;Kim, Sun-Min;Cha, Young-Ju
    • Proceedings of the Plant Resources Society of Korea Conference
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    • pp.104-104
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    • 2003
  • In this study, seven grain seeds(sorghum maize, buckwheat, soy bean, mung bean, red bean, and barngrass) and germinated seven grain seeds were examined the fibrinolytic activity through fibrin plate assay and SDS-PAGE. The results obtained were as follows : 1. In the fibrin plate assay, the extracts of maize, barngrass, sorghum and buckwheat showed fibrinolytic activity. Especially, Maize of them showed fibrinolytic activity that was almost similar to plasmin, fibrinolytic enzyme used as a positive control. 2. In the SDS-PAGE of seven grain seeds, fibrinolytic activity was remarkably shown in mung bean and red bean. 3. In the fibrin plate assay of germinated grain seeds, buckwheat(5 mm), buckwheat(10 mm) and soy bean(10 mm) showed a level of fibrinolytic activity that was about 0.3 fold than 1.0 unit of plasmin, Also maize(10 mm) of them showed a level of fibrinolytic activity that was about 0.5 fold than 1.0 unit of plasmin. As a result, maize of grain seeds was found that it has a strong fibrinolytic activity.

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Studies on Fibrinolytic Activity of Jujube (Zizyphus mauritiana) Extract (대추 추출물의 fibrinolytic activity에 관한 연구)

  • Lee Min-Kyung
    • Journal of Life Science
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    • v.16 no.2
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    • pp.357-359
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    • 2006
  • Crude extract prepared from jujube (Zizyphus mauritiana) possseses fibrinolytic activity hydrolyzing fibrin. A clear transparent region is observed where fibrin is hydrolyzed, and its diameter increased as the added jujube extract increased. The fibrinolytic activity of jujube extract seems to be heat and acid stable since its activity was retained after heat treatment at $100^{\circ}C$ for 10 min or an acid treatment by incubating at pH 2.0, 3.0, and 4.0 for 3 hours. But the jujube extract dialyzed with a cellulose membrane with molecular weight cutoff of 12,000 and 2,000 lost its activity, which suggests the fibrinolytic activity might be compounds of low molecular weight.

Screening and Imentification of the Fibinolytic Bacterial Strain from Chungkook-jang (청국장으로부터 혈전용해균주의 분리 및 동정)

  • 김용택;김원극;오훈일
    • Microbiology and Biotechnology Letters
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    • v.23 no.1
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    • pp.1-5
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    • 1995
  • Bacterial strains showing the fibrinolytic activity were screened from Chungkook-jang and Natto (Japanese traditional soy food). The strains isolated from Natto revealed a high level of fibrinolytic activity, wherease nearly half of the isolates from Chungkook-jang did not show the relevant activity. However, one strain isolated from Chungkook-jang showed the highest fibrinolytic activity (1.84 plasmin unit), and subsequently identified as Bacillus species. The fibrinolytic strain was designated as Bacillus sp. CK 11-4.

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Purification and Characterization of a Fibrinolytic Enzyme from Snake Venom of Macrovipera lebetina turanica

  • Kwon, Ki-Rok;Park, Do-Il;Lee, Seung-Bae;Choi, Suk-Ho
    • Journal of Pharmacopuncture
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    • v.14 no.2
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    • pp.5-14
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    • 2011
  • Objectives: Fibrinolytic enzyme preparations were isolated from the snake venom of Macrovipera lebetica turanica in this study. Methods: The purity of the preparations was determined using SDS-PAGE and the enzymic characteristics of the purified fibrinolytic enzyme were determined. Results: 1. All of the two preparations with fibrinolytic activity obtained from the snake venom of M. l. turanicat contained the major polypeptide with the molecular weight of 27,500. One of the preparation showed purified fibrinolytic enzyme. 2. The purified fibrinolytic enzyme hydrolyzed ${\alpha}$-chain of fibrinogen faster than ${\beta}$-chain but not ${\gamma}$-chain. 3. The fibrinolytic activity was inhibited completely by EDTA, EGTA, 1,10-phenanthroline, and dithiothreitol. 4. The fibrinolytic activity was inhibited completely by calcium chloride, iron(III) chloride, mercuric chloride, and cobalt (II) chloride. 5. The fibrinolysis zone formed after addition of zinc sulfate was smaller but clearer than the control. Conclusions: These results suggested that the fibrinolytic enzyme purifed from the snake venom of M. l turanica was a metalloprotease containing dithiol group.

Screening Test of Wild Mushroom Extracts for Fibrinolytic Activity

  • Kim, Jun-Ho
    • Biomedical Science Letters
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    • v.8 no.3
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    • pp.173-177
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    • 2002
  • To investigate the fibrinolytic activities of the Korean basidiomycetes, the Extracts of 50 wild mushrooms were tested for their fibrinolytic activites. Extract from Tricholoma sejunctum showed 175% increased activity to that of plasmin 1.0 U/ml. Marasmius siccus showed 54% of activity, and Laetiporus sulphureus var. miniatus and Macrolepiota procera, 43% and 26% activities, respectively to that of plasmin. But, Cystoderma amianthinum, Lepiota sp., Coprinus sp., Lycoperdon sp. were less than 10% of plasmin activity.

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Screening Test of Wild Mushroom Methanol Extracts for Fibrinolytic and $\alpha-Glucosidase$ Inhibitory Activity

  • Kim, Jun-Ho;Yoo, Kwan-Hee;Seok, Soon-Ja
    • Biomedical Science Letters
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    • v.13 no.3
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    • pp.245-249
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    • 2007
  • We investigated the fibrinolytic and ${\alpha}-glucosidase$ inhibitory activity of 55 wild mushroom methanol extracts. Among them, 14 mushrooms showed fibrinolytic activity. In particular, Amanita virgineoides showed the greatest enzyme activity (3.9 plasmin units/ml) by a fibrin plate assay. The fibrinolytic activities of Suillus pictus and Polypolellus varius were 3.8 plasmin units, and the activity of Gomphus fujisanensis was 2.8 plasmin units. Leccinum extremiorientale and Xerocomus nigromaculatus had the same activity with 2.3 plasmin units. In a ${\alpha}-glucosidase$ inhibitory activity test, Lactarius sp. showed the greatest inhibitory activity at 97.3%. The ${\alpha}-glucosidase$ inhibitory activities of Clitocybe odora, Xerocomus nigromaculatus, Melanoleuca melaleuca, Suillus pictus, and Gyroporus castaneus were 84.3%, 77.9%, 74.6%, 68.7%, and 65.4%, respectively. According to the results, because Suillus pictus and Xerocomus nigromaculatus have strong fibrinolytic and ${\alpha}-glucosidase$ inhibitory activities, the two mushrooms will be used as materials for the development of new biofunctional food.

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Optimization of the Production of Fibrinolytic Enzyme from Bacillus firmus NA-1 in Fermented Soybeans

  • Seo, Ji-Hyun;Lee, Sam-Pin
    • Preventive Nutrition and Food Science
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    • v.9 no.1
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    • pp.14-20
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    • 2004
  • Bacillus strains capable of producing fibrinolytic enzyme were isolated from traditional fermented Korean soybean paste and Japanese fermented soybean (Natto). Among the 16 strains, a selected Bacillus sp. was identified as bacillus firmus, with 80.7% homology, by API kit analysis. Seed starter or B. firmus NA-1 was prepared with 5% soymilk prepared from micronized soybean powder. To produce fibrinolytic enzyme by B. firmus NA-1 the liquid culture was performed with NB broth (pH 7.0) fortified with 1% galactose, 0.1% tryptone, and 0.5% $K_2$HPO$_4$, by shaking with 180 rpm at 37$^{\circ}C$. Fibrinolytic enzyme activity reached the highest value at 7.8 unit/mL (plasmin unit) after fermentation for 72 hr. The crude fibrinolytic enzyme showed higher relative activity in the range of pH 7.0∼9.0. The activity of crude fibrinolytic enzyme was well maintained even after concentration by the vacuum evaporation at 5$0^{\circ}C$ for 1 hr.

Purification and Characterization of Fibrinolytic Enzyme from Armillariella mellea (뽕나무버섯으로부터 Fibrinolytic enzyme의 정제 및 특성 연구)

  • Kim, Jun-Ho;Kim, Yang-Sun
    • The Korean Journal of Mycology
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    • v.26 no.4
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    • pp.583-588
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    • 1998
  • A fibrinolytic enzyme has been isolated from the edible honey mushroom, Armillariella mellea and purified. The apparent molecular mass of purified enzyme was estimated to be 19800Da by SDS polyacryl amide gel electrophoresis and 19900Da by gel filtration, indicating that it was a monomer. The enzyme was optimal at pH 7, suggesting that the purified enzyme was a neutral proteinase. It shows the maximum fibrinolytic activity at $55^{\circ}C$, is completely inactivated above $65^{\circ}C$, and still indicates 40% of activity at $37^{\circ}C$. The fibrinolytic activity has been decreased by the addition of EDTA. Fifteen amino acid sequence was determined by protein sequencing techniques.

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Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang

  • Kim, Gyoung-Min;Lee, Ae-Ran;Lee, Kang-Wook;Park, Ae-Yong;Chun, Ji-Yeon;Cha, Jae-Ho;Song, Young-Sun;Kim, Jeong-Hwan
    • Journal of Microbiology and Biotechnology
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    • v.19 no.9
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    • pp.997-1004
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    • 2009
  • Bacillus amyloliquefancies CH51 isolated from cheonggukjang, a traditional Korean fermented soy food, has strong fibrinolytic activity and produces several fibrinolytic enzymes. Among four different growth media, tryptic soy broth was the best in terms of supporting cell growth and fibrinolytic activity of this strain. A protein with fibrinolytic activity was partially purified from the culture supernatant by CM-Sephadex and Phenyl Sepharose column chromatographies. Tandem mass spectrometric analysis showed that this protein is a homolog of AprE from B. subtilis and it was accordingly named AprE51. The optimum pH and temperature for partially purified AprE51 activity were 6.0 and $45^{\circ}C$, respectively. A gene encoding AprE51, aprE51, was cloned from B. amyloliquefaciens CH51 genomic DNA. The aprE51 gene was overexpressed in heterologous B. subtilis strains deficient in fibrinolytic activity using an E. coli-Bacillus shuttle vector, pHY300PLK.

Characterization of Fibrinolytic Proteases from Gloydius blomhoffii siniticus Venom

  • Choi, Suk-Ho
    • Journal of Pharmacopuncture
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    • v.14 no.3
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    • pp.71-79
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    • 2011
  • Objectives : This study was undertaken to identify fibrinolytic proteases from Gloydius blomhoffii siniticus venom and to characterize a major fibrinolytic protease purified from the venom. Methods : The venom was subjected to chromatography using columns of Q-Sepharose and Sephadex G-75. The molecular weights of fibrinolytic proteases showing fibrinolytic zone in fibrin plate assay were determined in SDS-PAGE (Sodium dodecyl sulfate-polyacrylamide gel electrophoresis) The effects of inhibitors and metal ions on fibrinolytic protease and the proteolysis patterns of fibrinogen, gelatin, and bovine serum albumin were investigated. Results : 1) The fibrinolytic fractions of the three peaks isolated from Gloydius blomhoffii siniticus venom contained two polypeptides of 46 and 59 kDa and three polypeptides of 32, 18, and 15 kDa and a major polypeptide of 54 kDa, respectively. 2) The fibrinolytic activity of the purified protease of 54 kDA was inhibited by metal chelators, such as EDTA, EGTA, and 1,10-phenanthroline, and disulfhydryl-reducing compounds, such as dithiothreitol and cysteine. 3) Calcium chloride promoted the fibrinolytic activity of the protease, but mercuric chloride and cobalt(II) chloride inhibited it. 4) The fibrinolytic protease cleaved preferentially A${\alpha}$-chain and slowly B${\beta}$-chain of fibrinogen. It also hydrolyzed gelatin but not bovine serum albumin. Conclusions : The Gloydius blomhoffii siniticus venom contained more than three fibrinolytic proteases. The major fibrinolytic protease was a metalloprotease which hydrolyzed both fibrinogen and gelatin, but not bovine serum albumin.