Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis

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dc.contributor.authorChang Won Kho-
dc.contributor.authorSung Goo Park-
dc.contributor.authorS Cho-
dc.contributor.authorDo Hee Lee-
dc.contributor.authorP K Myung-
dc.contributor.authorByoung Chul Park-
dc.date.accessioned2017-04-19T09:02:02Z-
dc.date.available2017-04-19T09:02:02Z-
dc.date.issued2005-
dc.identifier.issn1046-5928-
dc.identifier.uri10.1016/j.pep.2004.08.008ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6764-
dc.description.abstractWe have previously reported a proteomic approach to detect fibrinolytic enzymes from the secreted proteins of Bacillus subtilis 168 and identified two extracellular fibrinolytic enzymes of Bacillus, namely, Vpr and WprA. In this study, to confirm the fibrinolytic activity of Vpr, we cloned the vpr gene and expressed it in Escherichia coli, where it is predominantly localized to inclusion bodies. After affinity purification and desalting steps, the expressed Vpr is auto-processed to an active form. Interestingly, after the desalting step, several additional bands with fibrinolytic activity were detected in zymography gel along with a mature form (68 kDa) of Vpr. MALDI-TOF analyses of these bands revealed that Vpr could exist in multiple forms.-
dc.publisherElsevier-
dc.titleConfirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis-
dc.title.alternativeConfirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis-
dc.typeArticle-
dc.citation.titleProtein Expression and Purification-
dc.citation.number1-
dc.citation.endPage7-
dc.citation.startPage1-
dc.citation.volume39-
dc.contributor.affiliatedAuthorChang Won Kho-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorDo Hee Lee-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.alternativeName고창원-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName명평근-
dc.contributor.alternativeName박병철-
dc.identifier.bibliographicCitationProtein Expression and Purification, vol. 39, no. 1, pp. 1-7-
dc.identifier.doi10.1016/j.pep.2004.08.008-
dc.subject.keywordFibrinolytic enzymes-
dc.subject.keywordMass spectrometry-
dc.subject.keywordSerine protease-
dc.subject.keywordVpr-
dc.subject.keywordZymography-
dc.subject.localFibrinolytic enzyme-
dc.subject.localFibrinolytic enzymes-
dc.subject.localfibrinolytic enzyme-
dc.subject.localMass spetrometry-
dc.subject.localMass spectrometry (MS)-
dc.subject.localmass spectrometry-
dc.subject.localMass spectrometry-
dc.subject.localmass spectrometry (MS)-
dc.subject.localSerine protease-
dc.subject.localserine protease-
dc.subject.localVpr-
dc.subject.localZymography-
dc.subject.localzymography-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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