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

  • Kho, CW; 
  • Park, SG; 
  • Cho, S; 
  • Lee, DH; 
  • Myung, PK; 
  • 외 1명
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초록

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.

키워드

serine protease; Vpr; zymography; mass spectrometry; fibrinolytic enzymes; SERINE PROTEASE; ZYMOGRAPHY; GENE; GELS; BACILLUS-SUBTILIS-168; METALLOPROTEASE; FORMS
제목
Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis
저자
Kho, CW; Park, SG; Cho, S; Lee, DH; Myung, PK; Park, BC
DOI
10.1016/j.pep.2004.08.008
발행일
2005-01
유형
Article
저널명
Protein Expression and Purification
권
39
호
1
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1 ~ 7