Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis
- Authors
- Kho, CW; Park, SG; Cho, S; Lee, DH; Myung, PK; Park, BC
- Issue Date
- Jan-2005
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- serine protease; Vpr; zymography; mass spectrometry; fibrinolytic enzymes
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, v.39, no.1, pp 1 - 7
- Pages
- 7
- Journal Title
- PROTEIN EXPRESSION AND PURIFICATION
- Volume
- 39
- Number
- 1
- Start Page
- 1
- End Page
- 7
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24689
- DOI
- 10.1016/j.pep.2004.08.008
- ISSN
- 1046-5928
1096-0279
- Abstract
- We have previously reported a proteomic approach to detect fibrinolytic enzymes from the secreted proteins of Bacillis 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. (C) 2004 Elsevier Inc. All rights reserved.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > ETC > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24689)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.