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

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Title
Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis
Author(s)
Chang Won Kho; Sung Goo Park; S Cho; Do Hee Lee; P K Myung; Byoung Chul Park
Bibliographic Citation
Protein Expression and Purification, vol. 39, no. 1, pp. 1-7
Publication Year
2005
Abstract
We 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.
Keyword
Fibrinolytic enzymesMass spectrometrySerine proteaseVprZymography
ISSN
1046-5928
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.pep.2004.08.008
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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