• Biomedical Science Letters
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• v.12 no.3
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• pp.225-231
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• 2006

Fibrinolytic enzyme was purified from the fruiting bodies of Lepista nuda, using DEAE-Cellulose chromatography, Phenyl Sepharose chromatography, and Mono-S column chromatography. The substance has a molecular weight of 30006.62 Da as measured by MALD-TOF mass spectrometry. The N-terminal amino acid sequence of the enzyme was Tyr-Pro-Ser-Pro-Ser-His-Gln-Thr-Ala-Val-Asn-Ala-Ile-Ile-X. The activity of the enzyme was inhibited by PMSF, indicating that the enzyme is a serine protease. No inhibition was found with E-64, pepstatin, and EDTA. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to $30^{\circ}C$. The enzyme hydrolyzes both Aa and y chains of human fibrinogen but did not show any reactivity for $B{\beta}$ chain of human fibrinogen.

• Biomedical Science Letters
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• v.16 no.4
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• pp.271-277
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• 2010

This study was conducted to investigate the biological activities of Areca catechu L. The antioxidative, fibrinolytic, thrombin inhibitory, and ${\alpha}$-glucosidase inhibitory activities of Areca catechu L extracted with hexane, $CHCl_3$, ethyl acetate, butanol, and water were measured. The water fraction showed the highest extraction yield at 3.65% (w/w). The butanol, $CHCl_3$, water, and ethyl acetate fractions showed strong antioxidative activities at 81.6%, 87.1%, 88.0%, and 89.5%, respectively. The fibrinolytic activity was strong only in the ethyl acetate fraction at 0.84 plasmin units/ml. The 100-fold dilution of the water fraction had the strongest thrombin inhibitory activity at 59.2%. The 100-fold dilution of butanol fraction displayed the strongest ${\alpha}$-glucosidase inhibitory activity at 88.6%. In conclusion, the extracts of Areca catechu L hold promise for use in the development of biofunctional foods to prevent cardiovascular diseases.

• International Journal of Vascular Biomedical Engineering
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• v.4 no.2
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• pp.13-18
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• 2006

Direct injection of a fibrinolytic agent to the intra-arterial thrombosis may increase the effectiveness of thrombolysis by enhancing the permeation of thrombolytic agents into the blood clot. Permeation of fibrinolytic agents into a clot is influenced by the surface pressure, which is determined by the injection velocity of fibrinolytic agents. Computational fluid dynamic methods were used in order to predict clot lysis for different jet velocities and nozzle arrangements. Firstly, thrombolysis of a clot was mathematically modeled based on the pressure and lysis front velocity relationship. Direct injection of a thrombolytic agent increased the speed of thrombolysis significantly and the effectiveness was increased as the ejecting velocity increased. The nine nozzles model showed about 20% increase of the lysed volume, and the one and seventeen nozzles models did not show significant differences. Secondly, thrombolysis was modeled based on the enzyme transport and the fluid flow equations, and quasi steady numerical analysis was performed. Clot lysis efficiency was also increased as injection velocity increased.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.675-678
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• 1999

Fibrinolytic protease activity was detected in the fruit body of Pleurotus sajor-caju using a fibrin plate method. Two fibrinolytic activities (FPI and Ⅱ) were found at the regions of 14.5 and 86.0 kDa by using gel-filtration column chromatography. FPⅡ was identified as an alkaline protease, whereas FPⅠ was a neutral protease. Both were inhibited by phenanthrolin and EDTA, suggesting that they are metalloprotease. Inactivated enzyme activities were restored by adding Co/sup 2+/ or Zn/sup 2+/. Iodoacetate inhibited FPⅠ, but not FPⅡ. Both enzymes cleaved B/sub β/ and γ chains of the human fibrinogen. FPⅡ showed a preference to hydrophobic and bulky residues of nitroanilidine compounds as substrates, whereas FPⅠ preferred positively charged residues.

• Biomedical Science Letters
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• v.8 no.4
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• pp.245-250
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• 2002

Fibrinolytic enzyme has been purified from the edible mushroom, Tricholoma sejunctum using DEAE-cellulose chromatography, Phenyl-Sepharose chromatography and Mono-S column chromatography. The apparent molecular mass of purified enzyme was estimated to be 17100 Da by SDS-polyacrylamide gel electrophoresis and 19000 Da by gel filtration, Indicating that it was a monomer. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. It has a pH optimum at pH 9.5, suggested that purified enzyme was a alkaline protease. The activity of purified enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that purified enzyme is a metalloprotease. The activity of purified enzyme was increased by Zn$^{2+}$ and Co$^{2+}$, however, the enzyme activity was totally inhibited by Hg$^{2+}$.

• Biomedical Science Letters
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• v.17 no.2
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• pp.157-165
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• 2011

In this study, we investigated the biological activities of Carthamus tinctorius including antioxidative, fibrinolytic, thrombin inhibitory, ${\alpha}$-glucosidase inhibitory and collagenase inhibitory activities. Carthamus tinctorius, hot water extract was fractionated into hexane, chloroform, ethyl acetate, butanol and water fraction. Each of these was assayed individually. The hot water extract showed high antioxidative activity and thrombin inhibitory activity at 90.17% and 97.10% respectively. In the fraction activity tests, chloroform fraction showed the highest antioxidative activity at 81.85%. The fibrinolytic activity was strong only in the butanol fraction at 0.70 plasmin units/ml. The thrombin inhibitory activities of hexane, ethyl acetate and butanol fractions were 97.35%, 86.74% and 93.18% respectively. In collagenase inhibitory activity test, hexane fraction showed the highest activity at 87.78%. In conclusion, the hot water extract and solvent fractions of Carthamus tinctorius L can be used as a material for the development of biofunctional tea and foods respectively.

• Journal of Microbiology and Biotechnology
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• v.22 no.2
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• pp.215-219
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• 2012

The strain KCTC 11629BP, isolated from spontaneously fermented pine needle extract (FPE), showed fibrinolysis activity. The isolated strain was analyzed in physiological and biochemical experiments. Based on 16S rDNA sequencing and phylogenic tree analysis, the strain was identified to be a part of the genus Acetobacter, with Acetobacter senegalensis and Acetobacter tropicalis as the closest phylogenetic neighbors. Based on genotypic and phenotypic results, it was proposed that bacterial strain KCTC 11629BP represents a species of the genus Acetobacter. The strain was thusly named Acetobacter sp. FP1. In conclusion, Acetobacter sp. FP1 isolated from FPE possesses fibrinolytic activity.

• Proceedings of the PSK Conference
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• 2002.10a
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• pp.394.1-394.1
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• 2002

A thrombus is a mass formed from the constituents of the blood within the vessels or the heart during life. The process of formation is known as thrombosis. A vegetable warms producing fibrinolytic enzyme was isolated from chines traditional medicinal mushrooms. Cordyceps militairs and Paecilomyces tenuipes. The fibrinolytic enzyme of Cordyceps militaris and Paecilomyces tenuipes was purified from fruiting body by -70 prechilled ethanol precipitation. ion-exchange chromatography. gel filtration. (omitted)

• Journal of Life Science
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• v.5 no.4
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• pp.203-210
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• 1995

Fibrinolytic activity of fermented kimchi and ingredients used for the preparation were assayed by measuring the lysis area on plasminogen-rich fibrin plate. Fermented kimchi and picked fish sauces from changlan, prwan, and anchovy showed the activity, and the activity of pickled fish sauces were high in the order of pickled changlan, picked anchovy(pickled mulchi), and pickled prawn. However, the activity of kimchi may not be attributed to pickled fish sauce because kimchi containing fish sauce did not possess activities were determined from the samples heated for 30min at 100$\circ$C. There was no changes in activities before and after heat treatment indicating the agents may be components other than protein. Since major changes occur during kimchi fermentation were increased sour taste due to production of organic acids such as lactic, citric, oxalic, and succinic acids, the authentic organic acids present were examined for fibrinolytic activities. The results indicates that the major component posses the activity is lactic acid.

• KSBB Journal
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• v.21 no.6 s.101
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• pp.433-438
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• 2006

A fibrinolytic enzyme gene (BCF-1) was subcloned to the pEB vector which is high expression vector in the Bacillus host. The enzyme was purified by using FPLC after ammonium sulfate precipitation. The enzyme was oral-administrated to the rat and checked the bleeding time, blood clotting time and fibrinolytic effect of the serum. In the bleeding time retardation test, it was longer about 1.7 fold in the feeding rat than without feeding. The serum of rat feeded with the enzyme had the fibrinolytic activity from 1 hour to 3 hours after oral-administration. After 3 hours from feeding, the fibrinolytic activity was decreased gradually. Also blood clotting time after bleeding was longer than that of control rat. The enzyme could be detected at band of 30,000 Da in the blood by western blotting. The enzyme was not harmful to the all internal organs of the rats. Taken together, the enzyme originated from B. subtilis BB-1 can be a candidate to develop the drug for thrombosis, arteriosclerosis and myocardial infarction.