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Fibrinolytic and Antiplatelet Aggregation Properties of a Recombinant Cheonggukjang Kinase

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dc.contributor.authorRadnaabazar, Chinzorig-
dc.contributor.authorPark, Chung Mu-
dc.contributor.authorKim, Jeong Hwan-
dc.contributor.authorCha, Jaeho-
dc.contributor.authorSong, Young-Sun-
dc.date.accessioned2022-12-27T03:04:40Z-
dc.date.available2022-12-27T03:04:40Z-
dc.date.issued2011-06-
dc.identifier.issn1096-620X-
dc.identifier.issn1557-7600-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/23702-
dc.description.abstractThis study characterized the efficacy of recombinant Cheonggukjang kinase (CGK) 3-5-rich fraction as a thrombolytic agent, which we overexpressed in Bacillus licheniformis ATCC10716, a strain normally lacking fibrinolytic activity. We found that CGK3-5 is a plasmin-like protease that directly degrades fibrin clots and does not activate plasminogen during fibrin clot lysis and platelet-rich clot lysis assays. We also confirmed antiplatelet and antithrombotic activity by CGK3-5-rich fraction both in vitro and in vivo. CGK3-5-rich fraction inhibited collagen-induced platelet aggregation in platelet-rich plasma in a concentration-dependent manner. The concentration of 1.5 mg/mL CGK3-5-rich fraction completely inhibited collagen-induced platelet aggregation. Furthermore, injection of CGK3-5-rich fraction into tail veins dose-dependently protected mice from death by pulmonary embolism induced by collagen and epinephrine. The survival rates were 30%, 70%, and 100%, respectively, with doses of 130 mg/kg, 260 mg/kg, and 520 mg/kg. These findings suggest that CGK3-5 holds promise as a treatment to mitigate the potentially effects of stroke and heart failure.-
dc.format.extent5-
dc.language영어-
dc.language.isoENG-
dc.publisherMARY ANN LIEBERT, INC-
dc.titleFibrinolytic and Antiplatelet Aggregation Properties of a Recombinant Cheonggukjang Kinase-
dc.typeArticle-
dc.publisher.location미국-
dc.identifier.doi10.1089/jmf.2010.1233-
dc.identifier.wosid000291015300009-
dc.identifier.bibliographicCitationJOURNAL OF MEDICINAL FOOD, v.14, no.6, pp 625 - 629-
dc.citation.titleJOURNAL OF MEDICINAL FOOD-
dc.citation.volume14-
dc.citation.number6-
dc.citation.startPage625-
dc.citation.endPage629-
dc.type.docTypeArticle-
dc.identifier.kciidART001564975-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaPharmacology & Pharmacy-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalResearchAreaNutrition & Dietetics-
dc.relation.journalWebOfScienceCategoryChemistry, Medicinal-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.relation.journalWebOfScienceCategoryNutrition & Dietetics-
dc.subject.keywordPlusBACILLUS-SUBTILIS-
dc.subject.keywordPlusDOEN-JANG-
dc.subject.keywordPlusENZYME-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusNATTOKINASE-
dc.subject.keywordPlusPLASMINOGEN-
dc.subject.keywordPlusSTAPHYLOKINASE-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusGENE-
dc.subject.keywordAuthorantiplatelet aggregation-
dc.subject.keywordAuthorantithrombotic activity-
dc.subject.keywordAuthorCheonggukjang kinase-
dc.subject.keywordAuthorplasmin-like protease-
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