• Title/Summary/Keyword: Fibrinolytic

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Characterization of Physiological Functionalities in Korean Traditional Liquors (전통 민속주의 생리기능성 탐색)

  • Kim, Jae-Ho;Lee, Dae-Hyung;Choi, Shin-Yang;Lee, Jong-Soo
    • Korean Journal of Food Science and Technology
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    • v.34 no.1
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    • pp.118-122
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    • 2002
  • Some physiological functionalities of Korean traditional liquors were characterized. Inhibitory activity against angiotensin-converting enzyme was 87.2% in Chunla-Do So-ju, 85.2% in Kyunggi-Do 2D-ju, and 85.9% in Chungcheong-Do DO-ju, Kyunggi-Do HO-ju, SA-ju, and Chunla-Do SO-ju had high fibrinolytic activity. SOD-like activity and electron donating ability were 70.7% in Kyunggi-Do OK-ju and 85.5% in Chungcheong-Do SA-ju, restectively. The highest tyrosinase inhibitory activity was shown in Kyungsang-Do KO-ju. High nitrite scavenging activity was detected in Chunla-Do To-ju.

Molecular Cloning, Sequencing, and Expression of a Fibrinolytic Serine-protease Gene from the Earthworm Lumbricus rubellus

  • Cho, Il-Hwan;Choi, Eui-Sung;Lee, Hyung-Hoan
    • BMB Reports
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    • v.37 no.5
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    • pp.574-581
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    • 2004
  • The full-length cDNA of the lumbrokinase fraction 6 (F6) protease gene of Lumbricus rubellus was amplified using an mRNA template, sequenced and expressed in E. coli cells. The F6 protease gene consisted of pro- and mature sequences by gene sequence analysis, and the protease was translated and modified into active mature polypeptide by N-terminal amino acid sequence analysis of the F6 protease. The pro-region of F6 protease consisted of the 44 residues from methionine-1 to lysine-44, and the mature polypeptide sequence (239 amino acid residues and one stop codon; 720 bp) started from isoleucine-45 and continued to the terminal residue. F6 protease gene clones having pro-mature sequence and mature sequence produced inclusion bodies in E. coli cells. When inclusion bodies were orally administrated rats, generated thrombus weight in the rat' venous was reduced by approximately 60% versus controls. When the inclusion bodies were solubilized in pepsin and/or trypsin solutions, the solubilized enzymes showed hemolytic activity in vitro. It was concluded the F6 protease has hemolytic activity, and that it is composed of pro- and mature regions.

Immobilization of Lum,brokinase on the Surface of Polyurethane by using the Photoreactive Poly(acrylic acid) (광반응성 poly(acrylic acid)를 이용한 Lumbrokinase 의 polyurethane 표면 고정화 방법에 관한 연구)

  • 김현정;류은숙;김종원;민병구
    • Journal of Biomedical Engineering Research
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    • v.20 no.6
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    • pp.547-553
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    • 1999
  • 생체재료로 사용되는 polyurethane(PU) 표면에 항혈전성 lumbrokinase(LK)를 고정함으로써 생체적합성을 향상시키고자하였다. 먼저 LK를 PU 표면에 고정하기 위한 가교제로서 4-azidoaniline hydrochloride와 poly(acrylic acid)를 이용하여 4-azidophenyl 작용기가 amido 결합으로 치환된 수용성, 광반응성 poly(acrylic acid)(PPa-II)를 합성하였다. H-nuclear magnetic reasonance spectrum(500MHz H-NMR)의 6-7 peak와 infrared spectrum (FT-IR) 의 2125.48 cm peak으로부터 PPA-II의 합성을 지원하였다. EH한 4-azidophenyl 작용기가 poly(acrylid acid) 잔기에 치환된 정도는 UV/VIS adpectrophotometric spectrum을 확인한 결과 11~14%임을 알 수있었다. 0.5 1및 5% PPA-II를 각각 광반응하여 얻은 PU는 39.5, 161.8 및 181.5 nmole/$\textrm{cm}^2$의 농도로 표면에 carvoxyl 작용기가 유도되었음을 알 수있었다. 0.05M KH2PO4 (pH 4.5) 용액에서 1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide(EDC)를 촉매로 사용하여 LK를 PU표면에 amido 공유결합으로 고정하였으며, 이것은 지속적인 fibrinolytic 활성도를 보였다. PPA-II를 이용한 표면 개질 방법은 수용성 반응조건에서 이루어진다는 점과 광반응을 이용함으로써 특정부위에서의 표면개질이 가능하다는 점에서 그 응용가치가 크며 아울러 PU의 생체적합성을 향상시킬 수 있는 방법으로서 판단된다.

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Quality Characteristics and Cardiovascular Activities of Korean Traditional Wines and Liquors

  • Yu, Hyung-Eun;Lee, Dae-Hyoung;Lee, Ju-Hyun;Choi, Sin-Yang;Lee, Jong-Soo
    • Food Science and Biotechnology
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    • v.14 no.6
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    • pp.772-777
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    • 2005
  • The goal of this study was to screen and characterize the physiological functions of Korean traditional wines (TW) and liquors (TL). Forty-two TW and TL were collected and evaluated for quality and cardiovascular activities. Ethanol content ranged from $9.0%{\sim}41%$, and pH ranged from $3.0{\sim}7.8$, and they also contained 0.01% to 0.67% of total acid. Samples contained a maximum of 2.0% of crude protein and $0.1%{\sim}14.0%$ of reducing sugar. Commercial CM-wine showed the highest antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity, 85.9%. The greatest fibrinolytic activity and platelet aggregation inhibitory activity were also found in commercial CM-wine (31.8U) and commercial SS2-wine (38.6 %), respectively. Commercial SHBI-liquor showed the highest HMG-CoA reductase inhibitory activity, 78%. The ACE inhibitor from commercial CM-wine was a peptide compound and also showed an antihypertensive effect in spontaneous hypertensive rats at a dosage of 1.5 mg/kg.

Physiological Functionality of Gugija Products and an In Vivo Examination on Anti-hypertension Effects (구기자 가공품의 생리기능성 및 항고혈압 활성 검증)

  • Lee, Ji-Su;Park, Young-Chun;Paik, Seung-Woo;Lee, Sox-Su;Ahn, Yong-Kun;Lee, Jong-Soo
    • The Korean Journal of Food And Nutrition
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    • v.21 no.2
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    • pp.115-120
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    • 2008
  • To develop a new Gugija(Lycium chinensis Mill) product having increased value, the physiological functionality of various commercial Gugija products were investigated. In addition, an in vivo study was performed using spontaneous hypertensive rats(SHR) to examine the anti-hypertension effects of products. The results showed that antioxidant activity was highest in the methanol extract of Gugija leaf pickle(97.7%), and anti-hypertensive angiotensin I -converting enzyme(ACE) inhibitory activity was 80.4% in Gugija doenjang(soybean paste) water extract. Anti-cholesterolemia HMG-CoA reductase inhibitory activity was highest in the methanol extract of Gugija rice cake(66.1 %). However, SOD-like activity was below 30% in most products; and fibrinolytic activity was not detected or was very weak. Ultimately, we selected Gugija tea and Gugija wine as superior anti-hypertensive Gugija products, and subsequent in vivo testing was performed using SHR, comparing the tea and wine to Gugija fruit. Among them, the Gugija fruit demonstrated the best anti-hypertension effects in SHR.

Protective Effects of a Novel Probiotic Strain of Lactobacillus plantarum JSA22 from Traditional Fermented Soybean Food Against Infection by Salmonella enterica Serovar Typhimurium

  • Eom, Jeong Seon;Song, Jin;Choi, Hye Sun
    • Journal of Microbiology and Biotechnology
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    • v.25 no.4
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    • pp.479-491
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    • 2015
  • Lactobacillus species have been shown to enhance intestinal epithelial barrier function, modulate host immune responses, and suppress the growth of pathogenic bacteria, yeasts, molds, and viruses. Thus, lactobacilli have been used as probiotics for treating various diseases, including intestinal disorders, and as biological preservatives in the food and agricultural industries. However, the molecular mechanisms used by lactobacilli to suppress pathogenic bacterial infections have been poorly characterized. We previously isolated Lactobacillus plantarum JSA22 from buckwheat sokseongjang, a traditional Korean fermented soybean food, which possessed high enzymatic, fibrinolytic, and broad-spectrum antimicrobial activity against foodborne pathogens. In this study, we investigated the effects of L. plantarum JSA22 on the growth of S. Typhimurium and S. Typhimurium-induced cytotoxicity by stimulating the host immune response in intestinal epithelial cells. The results showed that coincubation of S. Typhimurium and L. plantarum JSA22 with intestinal epithelial cells suppressed S. Typhimurium infection, S. Typhimurium-induced NF-κB activation, and IL-8 production, and lowered the phosphorylation of both Akt and p38. These data indicated that L. plantarum JSA22 has probiotic properties, and can inhibit S. Typhimurium infection of intestinal epithelial cells. Our findings can be used to develop therapeutic and prophylactic agents against pathogenic bacteria.

Relationship Between Acrylamide Concentration and Enzymatic Activity in An Improved Single Fibrin Zymogram Gel System

  • Choi, Nack-Shick;Kim, Byoung-Young;Lee, Jin-Young;Yoon, Kab-Seog;Han, Kyoung-Yoen;Kim, Seung-Ho
    • BMB Reports
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    • v.35 no.2
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    • pp.236-238
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    • 2002
  • Based on the zymography analysis, Bacillus sp. DJ-4 (screened from Doen-Jang, a Korean traditional fermented food) secretes seven extracellular fibrinolytic enzymes (EFEs; 68, 64, 55, 45, 33, 27, and 13 kDa) in culture broth. These seven EFEs were analyzed by newly applied SDS-fibrin zymography combined with gradient polyacrylamide (SDS-FZGP). This improved gel system was used with a 5-20% acrylamide gradient in a fibrin zymogram gel for the separation of proteins with molecular masses from below 10kDa to over 100kDa on one gel plate. Using this system, high molecular weight bands (HMWBs) were clearly and sharply resolved. We also examined the relationship between an acrylamide concentration and the enzymatic activity of EFE using densitometric analysis.

Screening of Thrombin Inhibitors from Medicinal and Wild Plants (약용 및 야생식물로부터 트롬빈 저해물질의 탐색)

  • Kwon, Yun-Sook;Kim, Young-Sook;Kwon, Ha-Young;Kwon, Gi-Seok;Kim, Kyung-Jae;Kwon, Chong-Suk;Son, Kun-Ho;Sohn, Ho-Yong
    • Korean Journal of Pharmacognosy
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    • v.35 no.1 s.136
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    • pp.52-61
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    • 2004
  • Inhibitory activities of 264 methanol extracts, which were prepared from different parts of 210 kinds of wild and medicinal plants, against human thrombin were evaluated. Based on the anti-coagulation activity determined by thrombin time and activated partial thromboplastin time, the 14 extracts were screened. The fibrinolytic activity, heat stability and inhibition of other proteolytic digestive enzymes, such as pepsin, papain, trypsin and chymotrypsin, of the 14 extracts were further determined, and Ginko biloba (herba), Ephedra sinica (radix), Reynoutria elliptica (herba), Amomum tsao-ko Crevost (fructus), and Magnolia officinalis Rehd. et Wils (bark) were finally selected as possible plant sources for anti-thrombosis agent. These results suggested that medicinal and wild plants could be the potential source of thrombin inhibitor.

Treatment of Severe Henoch-Schoenlein Purpura Nephritis in Children (소아의 심한 헤노흐-쇤라인 자반증의 치료)

  • Shin, Jae-Il;Lee, Jae-Seung
    • Childhood Kidney Diseases
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    • v.14 no.1
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    • pp.10-21
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    • 2010
  • The overall prognosis of Henoch-Schoenlein purpura (HSP) is favorable, but severe nephritis has a high risk of progression to end stage renal failure. Recent studies emphasize the importance of early treatment in children with severe HSP nephritis, but the treatment of severe HSP nephritis still remains controversial due to the rarity of randomized controlled studies in this field. Nevertheless, several intensive therapies, such as intravenous high-dose methylprednisolone pulse, immunosuppressive/cytotoxic drugs, fibrinolytic therapy, anticoagulants, antiplatelet agent and plasma exchange, have been used in children with severe HSP nephritis. In this review, we focus on the treatment of severe HSP nephritis in children.

Action of Extracellular Protease of Aspergillus terreus on Human Plasma Hemostasis Proteins

  • Alexander A. Osmolovskiy;Elena S. Zvonareva;Nina A. Baranova;Valeriana G. Kreyer
    • Microbiology and Biotechnology Letters
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    • v.51 no.2
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    • pp.167-173
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    • 2023
  • Proteolytic enzymes secreted by Aspergillus, as pathogenicity factors, affect blood coagulation and fibrinolysis, and therefore the target proteins of their action in the bloodstream are of significant interest. In the present study, the action of the isolated protease of A. terreus 2 on different human plasma proteins was shown. The protease of A. terreus 2 exhibited the highest proteolytic activity against hemoglobin, which was 2.5 times higher than the albuminolytic activity shown in both of the protein substrates used. In addition, the protease has significant ability to hydrolyze both fibrin and fibrinogen. However, the inability of the A. terreus 2 protease to coagulate rabbit blood plasma and coagulate human and bovine fibrinogen indicates the severity of the enzyme's action on human blood coagulation factors. It should be considered as a potential indicator of this isolated protease's participation in fungal pathogenesis. The protease shows no hemolytic activity. Furthermore, its activity is insignificantly inhibited by thrombin inhibitors, and is not inhibited by plasmin inhibitors.