Production of fibrinolytic enzyme in plastid-transformed tobacco plants

Cited 9 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorS M Ko-
dc.contributor.authorB H Yoo-
dc.contributor.authorJ M Lim-
dc.contributor.authorK H Oh-
dc.contributor.authorJ I Liu-
dc.contributor.authorSuk Weon Kim-
dc.contributor.authorJang Ryol Liu-
dc.contributor.authorK S Choi-
dc.contributor.authorE S Yoon-
dc.date.accessioned2017-04-19T09:15:36Z-
dc.date.available2017-04-19T09:15:36Z-
dc.date.issued2009-
dc.identifier.issn0735-9640-
dc.identifier.uri10.1007/s11105-009-0113-4ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9240-
dc.description.abstractThe earthworm fibrinolytic enzyme, which belongs to a group of serine proteases with strong fibrinolytic activity, has been used as an oral drug for prevention and treatment of thrombosis in East Asia. Fibrizyme is a fibrinolytic enzyme isolated from the earthworm Eisenia andrei. Here we report genetic engineering of tobacco plastids with stable integration of the fibrizyme gene into the tobacco chloroplast genome. A plastid transformation vector was constructed by introducing various regulatory elements into fibrizyme cDNA. This vector was delivered by particle bombardment into tobacco leaf explants and plastid-transformed plants were subsequently regenerated into whole plants through several rounds of selection. We confirmed stable integration of the fibrizyme gene into the tobacco plastid genome by PCR and Southern blot analyses. Northern and Western blot analyses revealed that mRNA and protein of recombinant fibrizyme were highly expressed in transformed tobacco plants.-
dc.publisherSpringer-
dc.titleProduction of fibrinolytic enzyme in plastid-transformed tobacco plants-
dc.title.alternativeProduction of fibrinolytic enzyme in plastid-transformed tobacco plants-
dc.typeArticle-
dc.citation.titlePlant Molecular Biology Reporter-
dc.citation.number4-
dc.citation.endPage453-
dc.citation.startPage448-
dc.citation.volume27-
dc.contributor.affiliatedAuthorSuk Weon Kim-
dc.contributor.affiliatedAuthorJang Ryol Liu-
dc.contributor.alternativeName고석민-
dc.contributor.alternativeName유병호-
dc.contributor.alternativeName임종민-
dc.contributor.alternativeName오광훈-
dc.contributor.alternativeName류재일-
dc.contributor.alternativeName김석원-
dc.contributor.alternativeName유장렬-
dc.contributor.alternativeName최관삼-
dc.contributor.alternativeName윤의수-
dc.identifier.bibliographicCitationPlant Molecular Biology Reporter, vol. 27, no. 4, pp. 448-453-
dc.identifier.doi10.1007/s11105-009-0113-4-
dc.subject.keywordBiopharmaceutical-
dc.subject.keywordChloroplast transformation-
dc.subject.keywordFibrinolytic enzyme-
dc.subject.keywordGenetically modified crops-
dc.subject.localBiopharmaceutical-
dc.subject.localbiopharmaceuticals-
dc.subject.localBiopharmaceuticals-
dc.subject.localbio-pharmaceutical-
dc.subject.localChloroplast transformation-
dc.subject.localFibrinolytic enzyme-
dc.subject.localFibrinolytic enzymes-
dc.subject.localfibrinolytic enzyme-
dc.subject.localGenetically modified (GM) crop-
dc.subject.localGenetically modified crop-
dc.subject.localGenetically modified crops-
dc.subject.localgenetically modifided crop-
dc.subject.localgenetically modified (GM) crop-
dc.subject.localgenetically modified crop-
dc.subject.localgenetically modified crops-
dc.description.journalClassY-
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.